1keq
From Proteopedia
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|PDB= 1keq |SIZE=350|CAPTION= <scene name='initialview01'>1keq</scene>, resolution 1.88Å | |PDB= 1keq |SIZE=350|CAPTION= <scene name='initialview01'>1keq</scene>, resolution 1.88Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=4MZ:4-METHYLIMIDAZOLE'>4MZ</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span> |
|GENE= MCA5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= MCA5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dmx|1DMX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1keq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1keq OCA], [http://www.ebi.ac.uk/pdbsum/1keq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1keq RCSB]</span> | ||
}} | }} | ||
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[[Category: Viola, R E.]] | [[Category: Viola, R E.]] | ||
[[Category: Wright, S K.]] | [[Category: Wright, S K.]] | ||
| - | [[Category: 4MZ]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: K]] | ||
| - | [[Category: ZN]] | ||
[[Category: engineered residue]] | [[Category: engineered residue]] | ||
[[Category: proton transfer]] | [[Category: proton transfer]] | ||
| - | ''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 21:47:31 2008'' |
Revision as of 18:47, 30 March 2008
| |||||||
| , resolution 1.88Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | MCA5C (Mus musculus) | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Related: | 1DMX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of F65A/Y131C Carbonic Anhydrase V, covalently modified with 4-chloromethylimidazole
Overview
The crystal structure of F65A/Y131C murine alpha-carbonic anhydrase V (CAV), covalently modified at cysteine residues with 4-chloromethylimidazole, is reported at 1.88 A resolution. This modification introduces a methylimidazole (MI) group at residue C131 in the active site with important consequences. F65A/Y131C-MI CAV exhibits an up to 3-fold enhancement of catalytic activity over that of wild-type CAV [Earnhardt, J. N., Wright, S. K., Qian, M., Tu, C., Laipis, P. J., Viola, R. E., and Silverman, D. N. (1999) Arch. Biochem. Biophys. 361, 264-270]. In this modified CAV variant, C131-MI acts as a proton shuttle, facilitating the deprotonation of a zinc-bound water molecule to regenerate the nucleophilic zinc-bound hydroxide ion. A network of three hydrogen-bonded water molecules, across which proton transfer likely proceeds, bridges the zinc-bound water molecule and the C131-MI imidazole group. The structure of F65A/Y131C-MI CAV is compared to structures of Y64H/F65A murine CAV, wild-type human alpha-carbonic anhydrase II, and the gamma-carbonic anhydrase from Methanosarcina thermophilain an effort to outline common features of catalytic proton shuttles.
About this Structure
1KEQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle., Jude KM, Wright SK, Tu C, Silverman DN, Viola RE, Christianson DW, Biochemistry. 2002 Feb 26;41(8):2485-91. PMID:11851394
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