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1w74

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==X-RAY STRUCTURE OF PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, PPIA, RV0009, FROM MYCOBACTERIUM TUBERCULOSIS.==
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<StructureSection load='1w74' size='340' side='right' caption='[[1w74]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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==X-ray structure of peptidyl-prolyl cis-trans isomerase A, PpiA, Rv0009, from Mycobacterium tuberculosis.==
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<StructureSection load='1w74' size='340' side='right'caption='[[1w74]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1w74]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W74 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1w74]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W74 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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=1w74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w74 OCA], [http://pdbe.org/1w74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w74 RCSB], [http://www.ebi.ac.uk/pdbsum/1w74 PDBsum]</span></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=1w74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w74 OCA], [https://pdbe.org/1w74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w74 RCSB], [https://www.ebi.ac.uk/pdbsum/1w74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w74 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIA_MYCTU PPIA_MYCTU] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:15479239</ref> <ref>PMID:17141764</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/1w74_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/1w74_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1w74 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
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*[[Cyclophilin|Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Myctu]]
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[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Henriksson, L M]]
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[[Category: Henriksson LM]]
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[[Category: Johansson, P]]
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[[Category: Johansson P]]
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[[Category: Mowbray, S L]]
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[[Category: Mowbray SL]]
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[[Category: Unge, T]]
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[[Category: Unge T]]
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[[Category: Cyclophilin]]
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[[Category: Isomerase]]
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[[Category: Peptidyl-prolyl cis-trans isomerase]]
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[[Category: Ppiase]]
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[[Category: Rotamase]]
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[[Category: Rv0009]]
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[[Category: Spine]]
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[[Category: Structural genomic]]
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[[Category: Structural proteomics in europe]]
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Current revision

X-ray structure of peptidyl-prolyl cis-trans isomerase A, PpiA, Rv0009, from Mycobacterium tuberculosis.

PDB ID 1w74

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