1kdz
From Proteopedia
(New page: 200px<br /><applet load="1kdz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdz, resolution 1.40Å" /> '''Pseudomonas Serine-C...) |
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| - | [[Image:1kdz.jpg|left|200px]]<br /><applet load="1kdz" size=" | + | [[Image:1kdz.jpg|left|200px]]<br /><applet load="1kdz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kdz, resolution 1.40Å" /> | caption="1kdz, resolution 1.40Å" /> | ||
'''Pseudomonas Serine-Carboxyl Proteinase Complexed with the Inhibitor Tyrostatin (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''<br /> | '''Pseudomonas Serine-Carboxyl Proteinase Complexed with the Inhibitor Tyrostatin (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. | + | Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make covalent bonds to the active site Ser287 through their aldehyde moieties, while their side chains occupy subsites S1-S4 of the enzyme. The mode of binding of the inhibitors is almost identical for their P1 and P2 side chains, while significant differences are observed for P3 and P4 (if present). Kinetic parameters for the binding of these nanomolar inhibitors to PSCP have been established and correlated with the observed mode of binding. The preferences of this enzyme for a larger side chain in P2 as well as Tyr or Phe in P1 are explained by the size, shape, and characteristics of the S2 and S1 regions of the protein structure, respectively. Networks of hydrogen bonds involving glutamic and aspartic acids have been analyzed for the atomic-resolution structure of the native enzyme. PSCP contains a calcium-binding site that consists of Asp328, Asp348, three amide carbonyl groups, and a water molecule, in almost perfect octahedral coordination. The presence of Ca(2+) cation is necessary for the activity of the enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1KDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xanthomonalisin Xanthomonalisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.101 3.4.21.101] Full crystallographic information is available from [http:// | + | 1KDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xanthomonalisin Xanthomonalisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.101 3.4.21.101] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Xanthomonalisin]] | [[Category: Xanthomonalisin]] | ||
[[Category: Dauter, Z.]] | [[Category: Dauter, Z.]] | ||
| - | [[Category: Dunn, B | + | [[Category: Dunn, B M.]] |
| - | [[Category: Glodfarb, N | + | [[Category: Glodfarb, N E.]] |
[[Category: Gustchina, A.]] | [[Category: Gustchina, A.]] | ||
[[Category: Li, M.]] | [[Category: Li, M.]] | ||
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[[Category: serine-carboxyl proteinase]] | [[Category: serine-carboxyl proteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:02 2008'' |
Revision as of 11:33, 21 February 2008
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Pseudomonas Serine-Carboxyl Proteinase Complexed with the Inhibitor Tyrostatin (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)
Overview
Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make covalent bonds to the active site Ser287 through their aldehyde moieties, while their side chains occupy subsites S1-S4 of the enzyme. The mode of binding of the inhibitors is almost identical for their P1 and P2 side chains, while significant differences are observed for P3 and P4 (if present). Kinetic parameters for the binding of these nanomolar inhibitors to PSCP have been established and correlated with the observed mode of binding. The preferences of this enzyme for a larger side chain in P2 as well as Tyr or Phe in P1 are explained by the size, shape, and characteristics of the S2 and S1 regions of the protein structure, respectively. Networks of hydrogen bonds involving glutamic and aspartic acids have been analyzed for the atomic-resolution structure of the native enzyme. PSCP contains a calcium-binding site that consists of Asp328, Asp348, three amide carbonyl groups, and a water molecule, in almost perfect octahedral coordination. The presence of Ca(2+) cation is necessary for the activity of the enzyme.
About this Structure
1KDZ is a Single protein structure of sequence from Pseudomonas sp. with as ligand. Active as Xanthomonalisin, with EC number 3.4.21.101 Full crystallographic information is available from OCA.
Reference
Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase., Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K, Biochemistry. 2001 Dec 25;40(51):15602-11. PMID:11747435
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