3g0m: Difference between revisions
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<StructureSection load='3g0m' size='340' side='right'caption='[[3g0m]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='3g0m' size='340' side='right'caption='[[3g0m]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3g0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3g0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G0M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=3g0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g0m OCA], [https://pdbe.org/3g0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g0m RCSB], [https://www.ebi.ac.uk/pdbsum/3g0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g0m ProSAT], [https://www.topsan.org/Proteins/CSGID/3g0m TOPSAN]</span></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=3g0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g0m OCA], [https://pdbe.org/3g0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g0m RCSB], [https://www.ebi.ac.uk/pdbsum/3g0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g0m ProSAT], [https://www.topsan.org/Proteins/CSGID/3g0m TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SUFE_SALTY SUFE_SALTY] Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process.[HAMAP-Rule:MF_01832] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: Anderson | [[Category: Anderson W]] | ||
[[Category: Joachimiak A]] | |||
[[Category: Joachimiak | [[Category: Maltseva N]] | ||
[[Category: Maltseva | [[Category: Nocek B]] | ||
[[Category: Nocek | [[Category: Stam J]] | ||
[[Category: Stam | |||
Latest revision as of 09:55, 6 September 2023
Crystal structure of cysteine desulfuration protein SufE from Salmonella typhimurium LT2Crystal structure of cysteine desulfuration protein SufE from Salmonella typhimurium LT2
Structural highlights
FunctionSUFE_SALTY Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process.[HAMAP-Rule:MF_01832] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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