2v3y
From Proteopedia
(New page: 200px<br /><applet load="2v3y" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v3y, resolution 1.60Å" /> '''HIS361ALA ESCHERICHI...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses | + | Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 2V3Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Sites: <scene name='pdbsite=AC1:Mn Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Mn Binding Site For Chain A'>AC2</scene> and <scene name='pdbsite=AC3:Cl Binding Site For Chain A'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3Y OCA]. | + | 2V3Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Sites: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3Y OCA]. |
==Reference== | ==Reference== | ||
| - | Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu., Graham SC, Guss JM, Arch Biochem Biophys. 2007 Oct 24 | + | Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu., Graham SC, Guss JM, Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17983589 17983589] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xaa-Pro aminopeptidase]] | [[Category: Xaa-Pro aminopeptidase]] | ||
| - | [[Category: Graham, S | + | [[Category: Graham, S C.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MN]] | [[Category: MN]] | ||
| Line 30: | Line 30: | ||
[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:03 2008'' |
Revision as of 16:53, 21 February 2008
|
HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT
Overview
Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed.
About this Structure
2V3Y is a Protein complex structure of sequences from Escherichia coli with and as ligands. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu., Graham SC, Guss JM, Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:17983589
Page seeded by OCA on Thu Feb 21 18:53:03 2008
