2jvw

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<StructureSection load='2jvw' size='340' side='right' caption='[[2jvw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2jvw' size='340' side='right' caption='[[2jvw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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[[2jvw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVW OCA]. <br>
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<table><tr><td colspan='2'>[[2jvw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aliivibrio_fischeri Aliivibrio fischeri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVW OCA]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VF0530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=668 Aliivibrio fischeri])</td></tr>
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<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jvw RCSB], [http://www.ebi.ac.uk/pdbsum/2jvw PDBsum], [http://www.topsan.org/Proteins/NESGC/2jvw TOPSAN]</span><br>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jvw RCSB], [http://www.ebi.ac.uk/pdbsum/2jvw PDBsum], [http://www.topsan.org/Proteins/NESGC/2jvw TOPSAN]</span></td></tr>
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<table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|right]]
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[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first structural representative from this protein domain family. We demonstrate that the structure of VF0530 adopts a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains. Moreover, gel shift binding data indicate a potential dsDNA binding role for VF0530. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first structural representative from this protein domain family. We demonstrate that the structure of VF0530 adopts a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains. Moreover, gel shift binding data indicate a potential dsDNA binding role for VF0530. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
== References ==
== References ==
<references/>
<references/>

Revision as of 09:58, 1 May 2014

Solution NMR structure of uncharacterized protein Q5E7H1 from Vibrio fischeri. Northeast Structural Genomics target VfR117

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