1zsb
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1ZSB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN and AZM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1ZSB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN and AZM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: ZN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZSB OCA]]. |
==Reference== | ==Reference== | ||
Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II., Huang, CC, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW, Biochemistry. 1996 Mar 19;35(11):3439-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8639494 8639494] | Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II., Huang, CC, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW, Biochemistry. 1996 Mar 19;35(11):3439-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8639494 8639494] | ||
| + | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:30:16 2007'' |
Revision as of 08:25, 30 October 2007
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CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE ANALOGUE ACETAZOLAMIDE
Overview
Direct metal ligands to transition metals in metalloproteins exert a, profound effect on protein-metal affinity and function. Indirect ligands, i.e., second-shell residues that hydrogen bond to direct metal ligands, typically exert more subtle effects on the chemical properties of the, protein-metal complex. However, E117 of human carbonic anhydrase II, (CAII), which is part of the E117-119-Zn(2+) triad, is a notable, exception: E117-substituted CAIIs exhibit dramatically increased kinetics, of zinc complexation, and the E117Q variant exhibits enormously diminished, catalytic activity and sulfonamide affinity. The three-dimensional, structures of zinc-bound and zinc-free E117Q CAII reveal no discrete, structural changes in the active site that are responsible for enhanced, zinc ... [(full description)]
About this Structure
1ZSB is a [Single protein] structure of sequence from [Homo sapiens] with ZN and AZM as [ligands]. Active as [Carbonate dehydratase], with EC number [4.2.1.1]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
Reference
Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II., Huang, CC, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW, Biochemistry. 1996 Mar 19;35(11):3439-46. PMID:8639494
Page seeded by OCA on Tue Oct 30 10:30:16 2007
Categories: Carbonate dehydratase | Homo sapiens | Single protein | Christianson, D.W. | Lesburg, C.A. | AZM | ZN | Acetylation | Lyase | Oxo-acid | Polymorphism | Zinc
