2k8i

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'''Unreleased structure'''
 
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The entry 2k8i is ON HOLD until Paper Publication
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==Solution structure of E.Coli SlyD==
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<StructureSection load='2k8i' size='340' side='right'caption='[[2k8i]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2k8i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K8I FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k8i OCA], [https://pdbe.org/2k8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k8i RCSB], [https://www.ebi.ac.uk/pdbsum/2k8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k8i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SLYD_ECOLI SLYD_ECOLI] Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins. The PPIase substrate specificity, carried out with synthetic peptides of the 'suc-Ala-Xaa-Pro-Phe-4NA' type (where Xaa is the AA tested), was found to be Phe > Ala > Leu.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</ref> Required for lysis of phiX174 infected cells by stabilizing the hydrophobic viral lysis protein E and allowing it to accumulate to the levels required to exert its lytic effect. May act by a chaperone-like mechanism.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</ref> Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/2k8i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2k8i ConSurf].
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<div style="clear:both"></div>
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Authors: Weininger, U., Balbach, J.
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==See Also==
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
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Description: Solution structure of E.Coli SlyD
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== References ==
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<references/>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 8 09:13:25 2008''
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Balbach J]]
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[[Category: Weininger U]]

Current revision

Solution structure of E.Coli SlyD

PDB ID 2k8i

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