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==Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S==
==Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S==
<StructureSection load='4g2p' size='340' side='right' caption='[[4g2p]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='4g2p' size='340' side='right'caption='[[4g2p]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g2p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._14028s Salmonella enterica subsp. enterica serovar typhimurium str. 14028s]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G2P FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._14028S Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G2P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">surA, STM14_0111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=588858 Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S])</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=4g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2p OCA], [https://pdbe.org/4g2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g2p RCSB], [https://www.ebi.ac.uk/pdbsum/4g2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g2p ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g2p RCSB], [http://www.ebi.ac.uk/pdbsum/4g2p PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/D0ZJR9_SALT1 D0ZJR9_SALT1]] Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (By similarity).[HAMAP-Rule:MF_01183]  
[https://www.uniprot.org/uniprot/A0A0F6AWM7_SALT1 A0A0F6AWM7_SALT1] Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.[HAMAP-Rule:MF_01183]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. 14028s]]
[[Category: Large Structures]]
[[Category: Adkins, J N]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]]
[[Category: Brown, R N]]
[[Category: Adkins JN]]
[[Category: Chang, C]]
[[Category: Brown RN]]
[[Category: Cort, J R]]
[[Category: Chang C]]
[[Category: Heffron, F]]
[[Category: Cort JR]]
[[Category: Jedrzejczak, R]]
[[Category: Heffron F]]
[[Category: Joachimiak, A]]
[[Category: Jedrzejczak R]]
[[Category: Structural genomic]]
[[Category: Joachimiak A]]
[[Category: Nakayasu, E S]]
[[Category: Nakayasu ES]]
[[Category: PCSEP, Program for the Characterization of Secreted Effector Proteins]]
[[Category: Wu R]]
[[Category: Wu, R]]
[[Category: Isomerase]]
[[Category: Mcsg]]
[[Category: Pcsep]]
[[Category: Program for the characterization of secreted effector protein]]
[[Category: Psi-biology]]

Latest revision as of 08:22, 6 December 2023

Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S

4g2p, resolution 1.82Å

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