This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2jvw
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
<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 == | ||
| - | [[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> | + | <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> |
| - | <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>< | + | </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> |
| - | <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>< | + | <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> |
| + | <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> | ||
| + | <table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| Line 15: | Line 17: | ||
</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> | ||
| + | <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. | ||
| Line 21: | Line 24: | ||
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> | ||
| + | </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
| |||||||||||
Categories: Aliivibrio fischeri | Acton, T B. | Aramini, J M. | Baran, M C. | Liu, J. | Montelione, G T. | NESG, Northeast Structural Genomics Consortium. | Nwosu, C. | Owens, L A. | Rossi, P. | Rost, B. | Swapna, G V.T. | Wang, D. | Xiao, R. | Alpha helical protein | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi-2 | Solution nmr structure | Structural genomic | Unknown function
