1cp6: Difference between revisions
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|PDB= 1cp6 |SIZE=350|CAPTION= <scene name='initialview01'>1cp6</scene>, resolution 1.9Å | |PDB= 1cp6 |SIZE=350|CAPTION= <scene name='initialview01'>1cp6</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BUB:1-BUTANE+BORONIC+ACID'>BUB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cp6 OCA], [http://www.ebi.ac.uk/pdbsum/1cp6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cp6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Petsko, G A.]] | [[Category: Petsko, G A.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:55 2008'' | ||
Revision as of 19:25, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE
OverviewOverview
Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report the X-ray crystal structure at 1.9 A resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents a snapshot of the proteolytic reaction in an arrested form between the Michaelis complex and the transition state. Comparison of the structure with spectroscopic and other data allows us to conclude that the apparently structurally symmetrical dizinc site is actually asymmetric electrostatically.
About this StructureAbout this Structure
1CP6 is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.
ReferenceReference
1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development., De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GA, Biochemistry. 1999 Jul 13;38(28):9048-53. PMID:10413478
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