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<PubmedArticle><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30190128</PMID><DateCompleted><Year>2019</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>504</Volume><Issue>1</Issue><PubDate><Year>2018</Year><Month>Sep</Month><Day>26</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of Escherichia&#x2002;coli DEAH/RHA helicase HrpB.</ArticleTitle><Pagination><StartPage>334</StartPage><EndPage>339</EndPage><MedlinePgn>334-339</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2018.08.191</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(18)31891-6</ELocationID><Abstract><AbstractText>RNA helicases are almost ubiquitous important enzymes that take part in multiple aspects of RNA metabolism. Prokaryotes encode fewer RNA helicases than eukaryotes, suggesting that individual prokaryotic RNA helicases may take on multiple roles. The specific functions and molecular mechanisms of bacterial DEAH/RHA helicases are poorly understood, and no structures are available of these bacterial enzymes. Here, we report the first crystal structure of the DEAH/RHA helicase HrpB of Escherichia coli in a complex with ADP&#x2022;AlF<sub>4</sub>. It showed an atypical globular structure, consisting of two RecA domains, an HA2 domain and an OB domain, similar to eukaryotic DEAH/RHA helicases. Notably, it showed a unique C-terminal extension that has never been reported before. Activity assays indicated that EcHrpB binds RNA but not DNA, and does not exhibit unwinding activity in&#xa0;vitro. Thus, within cells, the EcHrpB may function in helicase activity-independent RNA metabolic processes.</AbstractText><CopyrightInformation>Copyright &#xa9; 2018 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xin</LastName><ForeName>Ben-Ge</ForeName><Initials>BG</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Northwest A&amp;F University, Yangling, Shaanxi, 712100, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Wei-Fei</ForeName><Initials>WF</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Northwest A&amp;F University, Yangling, Shaanxi, 712100, China. Electronic address: weifei_c@nwsuaf.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rety</LastName><ForeName>Stephane</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Univ. Lyon, ENS de Lyon, Univ. Claude Bernard, CNRS UMR 5239, INSERM U1210, LBMC, 46 all&#xe9;e d'Italie Site Jacques Monod, F-69007, Lyon, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dai</LastName><ForeName>Yang-Xue</ForeName><Initials>YX</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Northwest A&amp;F University, Yangling, Shaanxi, 712100, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xi</LastName><ForeName>Xu-Guang</ForeName><Initials>XG</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Northwest A&amp;F University, Yangling, Shaanxi, 712100, China; LBPA, ENS de Cachan, Universit&#xe9; Paris-Saclay, Centre National de la Recherche Scientifique, 61 Avenue du Pr&#xe9;sident Wilson, 94235, Cachan, France. Electronic address: xxi01@ens-cachan.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009696">Nucleic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009711">Nucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>61D2G4IYVH</RegistryNumber><NameOfSubstance UI="D000244">Adenosine Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000244" MajorTopicYN="N">Adenosine Diphosphate</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009696" MajorTopicYN="N">Nucleic Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009711" MajorTopicYN="N">Nucleotides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Crystal structure</Keyword><Keyword MajorTopicYN="N">DEAH/RHA helicases</Keyword><Keyword MajorTopicYN="N">HrpB</Keyword><Keyword MajorTopicYN="N">RNA helicase</Keyword><Keyword MajorTopicYN="N">Sequence motif</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>8</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>8</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>9</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>3</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>9</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30190128</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2018.08.191</ArticleId><ArticleId IdType="pii">S0006-291X(18)31891-6</ArticleId></ArticleIdList></PubmedData></PubmedArticle></PubmedArticleSet>