View source for 1nxi


==Solution structure of Vibrio cholerae protein VC0424==
<StructureSection load='1nxi' size='340' side='right'caption='[[1nxi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nxi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NXI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxi OCA], [https://pdbe.org/1nxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nxi RCSB], [https://www.ebi.ac.uk/pdbsum/1nxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nxi ProSAT], [https://www.topsan.org/Proteins/NESGC/1nxi TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KUU1_VIBCH Q9KUU1_VIBCH] Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome (By similarity).[HAMAP-Rule:MF_01888]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/1nxi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1nxi ConSurf].
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== Publication Abstract from PubMed ==
The structure of Vibrio cholerae protein VC0424 was determined by NMR spectroscopy. VC0424 belongs to a conserved family of bacterial proteins of unknown function (COG 3076). The structure has an alpha-beta sandwich architecture consisting of two layers: a four-stranded antiparallel beta-sheet and three side-by-side alpha-helices. The secondary structure elements have the order alphabetaalphabetabetaalphabeta along the sequence. This fold is the same as the ferredoxin-like fold, except with an additional long N-terminal helix, making it a variation on this common motif. A cluster of conserved surface residues on the beta-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.

Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.,Ramelot TA, Ni S, Goldsmith-Fischman S, Cort JR, Honig B, Kennedy MA Protein Sci. 2003 Jul;12(7):1556-61. PMID:12824501<ref>PMID:12824501</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Cort JR]]
[[Category: Goldsmith-Fischman S]]
[[Category: Honig B]]
[[Category: Kennedy MA]]
[[Category: Ni S]]
[[Category: Ramelot TA]]