1i6p
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1i6p.jpg|left|200px]] | + | [[Image:1i6p.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)''' | + | {{Structure |
| + | |PDB= 1i6p |SIZE=350|CAPTION= <scene name='initialview01'>1i6p</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <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] | ||
| + | |GENE= YADF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1I6P is a [ | + | 1I6P 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=1I6P OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity., Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY, Protein Sci. 2001 May;10(5):911-22. PMID:[http:// | + | Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity., Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY, Protein Sci. 2001 May;10(5):911-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11316870 11316870] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 27: | Line 36: | ||
[[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 11:46:11 2008'' |
Revision as of 09:46, 20 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | YADF (Escherichia coli) | ||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)
Overview
Carbonic anhydrases fall into three distinct evolutionary and structural classes: alpha, beta, and gamma. The beta-class carbonic anhydrases (beta-CAs) are widely distributed among higher plants, simple eukaryotes, eubacteria, and archaea. We have determined the crystal structure of ECCA, a beta-CA from Escherichia coli, to a resolution of 2.0 A. In agreement with the structure of the beta-CA from the chloroplast of the red alga Porphyridium purpureum, the active-site zinc in ECCA is tetrahedrally coordinated by the side chains of four conserved residues. These results confirm the observation of a unique pattern of zinc ligation in at least some beta-CAS: The absence of a water molecule in the inner coordination sphere is inconsistent with known mechanisms of CA activity. ECCA activity is highly pH-dependent in the physiological range, and its expression in yeast complements an oxygen-sensitive phenotype displayed by a beta-CA-deletion strain. The structural and biochemical characterizations of ECCA presented here and the comparisons with other beta-CA structures suggest that ECCA can adopt two distinct conformations displaying widely divergent catalytic rates.
About this Structure
1I6P is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity., Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY, Protein Sci. 2001 May;10(5):911-22. PMID:11316870
Page seeded by OCA on Thu Mar 20 11:46:11 2008
