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==Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.== | ==Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.== | ||
<StructureSection load='2ph0' size='340' side='right' caption='[[2ph0]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2ph0' size='340' side='right'caption='[[2ph0]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ph0]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ph0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_carotovorus"_jones_1901 "bacillus carotovorus" jones 1901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PH0 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ovi|2ovi]], [[2hqv|2hqv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ovi|2ovi]], [[2hqv|2hqv]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECA3008 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECA3008 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=554 "Bacillus carotovorus" Jones 1901])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ph0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ph0 OCA], [https://pdbe.org/2ph0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ph0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ph0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ph0 ProSAT], [https://www.topsan.org/Proteins/NESGC/2ph0 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 33: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus carotovorus jones 1901]] | [[Category: Bacillus carotovorus jones 1901]] | ||
[[Category: Large Structures]] | |||
[[Category: Acton, T]] | [[Category: Acton, T]] | ||
[[Category: Chen, C X]] | [[Category: Chen, C X]] | ||
Latest revision as of 18:23, 17 June 2021
Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.Crystal structure of the Q6D2T7_ERWCT protein from Erwinia carotovora. NESG target EwR41.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report here the crystal structure at 2.0 A resolution of the AGR_C_4470p protein from the Gram-negative bacterium Agrobacterium tumefaciens. The protein is a tightly associated dimer, each subunit of which bears strong structural homology with the two domains of the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. Remarkably, the organization of the AGR_C_4470p dimer is the same as that of the two domains in ChuS and HemS, providing structural evidence that these two proteins evolved by gene duplication. However, the binding site for heme, while conserved in HemS and ChuS, is not conserved in AGR_C_4470p, suggesting that it probably has a different function. This is supported by the presence of two homologs of AGR_C_4470p in E. coli, in addition to the ChuS protein. Crystal structure of AGR_C_4470p from Agrobacterium tumefaciens.,Vorobiev SM, Neely H, Seetharaman J, Ma LC, Xiao R, Acton TB, Montelione GT, Tong L Protein Sci. 2007 Mar;16(3):535-8. PMID:17322535[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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