The X-ray Structure of Escherichia coli RraA (MenG), A Protein Inhibitor of RNA Processing
The Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing in vivo and in vitro. Here, we report the 2.0 Å X-ray structure of Rr...
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| Veröffentlicht in: | Journal of molecular biology 2003-10, Vol.332 (5), p.1015-1024 |
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| creator | Monzingo, Arthur F. Gao, Junjun Qiu, Ji Georgiou, George Robertus, Jon D. |
| description | The
Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a
trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing
in vivo and
in vitro. Here, we report the 2.0
Å X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12
Å in diameter. Based on earlier sequence analysis, RraA had been identified as a putative
S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the
E.
coli
RraA exhibits an ancient relationship to a family of aldolases. |
| doi_str_mv | 10.1016/S0022-2836(03)00970-7 |
| format | Article |
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Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a
trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing
in vivo and
in vitro. Here, we report the 2.0
Å X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12
Å in diameter. Based on earlier sequence analysis, RraA had been identified as a putative
S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the
E.
coli
RraA exhibits an ancient relationship to a family of aldolases.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/S0022-2836(03)00970-7</identifier><identifier>PMID: 14499605</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Aldehyde-Lyases - chemistry ; Amino Acid Sequence ; crystal structure ; Crystallography, X-Ray ; Databases as Topic ; degradosome ; disulfide bond formation ; Disulfides ; Endoribonucleases - metabolism ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium tuberculosis - metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA - chemistry ; Sequence Homology, Amino Acid ; three-layer sandwich</subject><ispartof>Journal of molecular biology, 2003-10, Vol.332 (5), p.1015-1024</ispartof><rights>2003 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-26748cea18d22e358426c7a266e55317d154e06162975dcde0dcc7037425bc423</citedby><cites>FETCH-LOGICAL-c392t-26748cea18d22e358426c7a266e55317d154e06162975dcde0dcc7037425bc423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0022-2836(03)00970-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14499605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Monzingo, Arthur F.</creatorcontrib><creatorcontrib>Gao, Junjun</creatorcontrib><creatorcontrib>Qiu, Ji</creatorcontrib><creatorcontrib>Georgiou, George</creatorcontrib><creatorcontrib>Robertus, Jon D.</creatorcontrib><title>The X-ray Structure of Escherichia coli RraA (MenG), A Protein Inhibitor of RNA Processing</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The
Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a
trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing
in vivo and
in vitro. Here, we report the 2.0
Å X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12
Å in diameter. Based on earlier sequence analysis, RraA had been identified as a putative
S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the
E.
coli
RraA exhibits an ancient relationship to a family of aldolases.</description><subject>Aldehyde-Lyases - chemistry</subject><subject>Amino Acid Sequence</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Databases as Topic</subject><subject>degradosome</subject><subject>disulfide bond formation</subject><subject>Disulfides</subject><subject>Endoribonucleases - metabolism</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mycobacterium tuberculosis - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>RNA - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>three-layer sandwich</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtrGzEUhUVpaBynP6FFq5JAJrmSRo9ZFRPyMDhJiR0I3YjxnetaxZ5JpZmA_338ollmdRf3O-fAx9g3AecChLkYA0iZSafMCahTgMJCZj-xngBXZM4o95n1_iOH7CilvwCgVe6-sEOR50VhQPfY78mc-HMWyxUft7HDtovEmxm_SjinGHAeSo7NIvDHWA74yR3VN6dnfMB_xaalUPNhPQ_T0DZxE3q83z6QUgr1n2N2MCsXib7ub589XV9NLm-z0cPN8HIwylAVss2ksblDKoWrpCSlXS4N2lIaQ1orYSuhcwIjjCysrrAiqBAtKJtLPcVcqj77set9ic2_jlLrlyEhLRZlTU2XvNWmsM6aD0HhXOGksmtQ70CMTUqRZv4lhmUZV16A39j3W_t-o9aD8lv7fpP7vh_opkuq3lN73Wvg5w6gtY_XQNEnDFQjVSEStr5qwgcTb162kQA</recordid><startdate>20031003</startdate><enddate>20031003</enddate><creator>Monzingo, Arthur F.</creator><creator>Gao, Junjun</creator><creator>Qiu, Ji</creator><creator>Georgiou, George</creator><creator>Robertus, Jon D.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20031003</creationdate><title>The X-ray Structure of Escherichia coli RraA (MenG), A Protein Inhibitor of RNA Processing</title><author>Monzingo, Arthur F. ; Gao, Junjun ; Qiu, Ji ; Georgiou, George ; Robertus, Jon D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-26748cea18d22e358426c7a266e55317d154e06162975dcde0dcc7037425bc423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aldehyde-Lyases - chemistry</topic><topic>Amino Acid Sequence</topic><topic>crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Databases as Topic</topic><topic>degradosome</topic><topic>disulfide bond formation</topic><topic>Disulfides</topic><topic>Endoribonucleases - metabolism</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mycobacterium tuberculosis - metabolism</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>RNA - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>three-layer sandwich</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Monzingo, Arthur F.</creatorcontrib><creatorcontrib>Gao, Junjun</creatorcontrib><creatorcontrib>Qiu, Ji</creatorcontrib><creatorcontrib>Georgiou, George</creatorcontrib><creatorcontrib>Robertus, Jon D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Monzingo, Arthur F.</au><au>Gao, Junjun</au><au>Qiu, Ji</au><au>Georgiou, George</au><au>Robertus, Jon D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The X-ray Structure of Escherichia coli RraA (MenG), A Protein Inhibitor of RNA Processing</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2003-10-03</date><risdate>2003</risdate><volume>332</volume><issue>5</issue><spage>1015</spage><epage>1024</epage><pages>1015-1024</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The
Escherichia coli protein regulator of RNase E activity A (RraA) has recently been shown to act as a
trans-acting modulator of RNA turnover in bacteria; it binds to the essential endonuclease RNase E and inhibits RNA processing
in vivo and
in vitro. Here, we report the 2.0
Å X-ray structure of RraA. The structure reveals a ring-like trimer with a central cavity of approximately 12
Å in diameter. Based on earlier sequence analysis, RraA had been identified as a putative
S-adenosylmethionine:2-demethylmenaquinone and was annotated as MenG. However, an analysis of the RraA structure shows that the protein lacks the structural motifs usually required for methylases. Comparison of the observed fold with that of other proteins (and domains) suggests that the RraA fold is an ancient platform that has been adapted for a wide range of functions. An analysis of the amino acid sequence shows that the
E.
coli
RraA exhibits an ancient relationship to a family of aldolases.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>14499605</pmid><doi>10.1016/S0022-2836(03)00970-7</doi><tpages>10</tpages></addata></record> |
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| issn | 0022-2836 1089-8638 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Aldehyde-Lyases - chemistry Amino Acid Sequence crystal structure Crystallography, X-Ray Databases as Topic degradosome disulfide bond formation Disulfides Endoribonucleases - metabolism Escherichia coli - metabolism Escherichia coli Proteins - chemistry Models, Molecular Molecular Sequence Data Mycobacterium tuberculosis - metabolism Protein Binding Protein Folding Protein Structure, Secondary Protein Structure, Tertiary RNA - chemistry Sequence Homology, Amino Acid three-layer sandwich |
| title | The X-ray Structure of Escherichia coli RraA (MenG), A Protein Inhibitor of RNA Processing |
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