2esf
From Proteopedia
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| - | [[Image:2esf.gif|left|200px]] | + | [[Image:2esf.gif|left|200px]] |
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| - | '''Identification of a Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial beta-Carbonic Anhydrase''' | + | {{Structure |
| + | |PDB= 2esf |SIZE=350|CAPTION= <scene name='initialview01'>2esf</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BCT:BICARBONATE ION'>BCT</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] | ||
| + | |GENE= can, cynT2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Identification of a Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial beta-Carbonic Anhydrase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ESF is a [ | + | 2ESF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESF OCA]. |
==Reference== | ==Reference== | ||
| - | Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase., Cronk JD, Rowlett RS, Zhang KY, Tu C, Endrizzi JA, Lee J, Gareiss PC, Preiss JR, Biochemistry. 2006 Apr 11;45(14):4351-61. PMID:[http:// | + | Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase., Cronk JD, Rowlett RS, Zhang KY, Tu C, Endrizzi JA, Lee J, Gareiss PC, Preiss JR, Biochemistry. 2006 Apr 11;45(14):4351-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16584170 16584170] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: zinc coordination]] | [[Category: zinc coordination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:43:51 2008'' |
Revision as of 14:43, 20 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | can, cynT2 (Escherichia coli) | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Identification of a Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial beta-Carbonic Anhydrase
Overview
The structures of beta class carbonic anhydrases (beta-CAs) determined so far fall into two distinct subclasses based on the observed coordination of the catalytic zinc (Zn2+) ion. The subclass of beta-CAs that coordinate Zn2+ tetrahedrally with four protein-derived ligands is represented by the structures of orthologues from Porphyridium purpureum, Escherichia coli, and Mycobacterium tuberculosis. Here we present the structure of an additional member of that subclass, that from Haemophilus influenzae, as well as detailed kinetic analysis, revealing the correspondence between structural classification and kinetic profile for this subclass. In addition, we identify a unique, noncatalytic binding mode for the substrate bicarbonate that occurs in both the H. influenzae and E. coli enzymes. The kinetic and structural analysis indicates that binding of bicarbonate in this site of the enzyme may modulate its activity by influencing a pH-dependent, cooperative transition between active and inactive forms. We hypothesize that the two structural subclasses of beta-CAs may provide models for the proposed active and inactive forms of the H. influenzae and E. coli enzymes.
About this Structure
2ESF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase., Cronk JD, Rowlett RS, Zhang KY, Tu C, Endrizzi JA, Lee J, Gareiss PC, Preiss JR, Biochemistry. 2006 Apr 11;45(14):4351-61. PMID:16584170
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