2m2a
From Proteopedia
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==NMR solution structure of the two domain PPIase SlpA from Escherichia coli== | ==NMR solution structure of the two domain PPIase SlpA from Escherichia coli== | ||
<StructureSection load='2m2a' size='340' side='right' caption='[[2m2a]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2m2a' size='340' side='right' caption='[[2m2a]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[2m2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M2A FirstGlance]. <br> | <table><tr><td colspan='2'>[[2m2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M2A FirstGlance]. <br> | ||
</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> | </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> | ||
| - | <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=2m2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2a OCA], [http://pdbe.org/2m2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m2a RCSB], [http://www.ebi.ac.uk/pdbsum/2m2a PDBsum]</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=2m2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2a OCA], [http://pdbe.org/2m2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m2a RCSB], [http://www.ebi.ac.uk/pdbsum/2m2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m2a ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FKBX_ECOLI FKBX_ECOLI]] PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln. | [[http://www.uniprot.org/uniprot/FKBX_ECOLI FKBX_ECOLI]] PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln. | ||
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| + | ==See Also== | ||
| + | *[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 22:48, 9 August 2018
NMR solution structure of the two domain PPIase SlpA from Escherichia coli
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