2a8c
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2a8c.gif|left|200px]] | [[Image:2a8c.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2a8c", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_2a8c| PDB=2a8c | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Haemophilus influenzae beta-carbonic anhydrase''' | '''Haemophilus influenzae beta-carbonic anhydrase''' | ||
Line 34: | Line 31: | ||
[[Category: Tu, C.]] | [[Category: Tu, C.]] | ||
[[Category: Zhang, K Y.J.]] | [[Category: Zhang, K Y.J.]] | ||
- | [[Category: | + | [[Category: Carbonic anhydrase]] |
- | [[Category: | + | [[Category: X-ray structure]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:44:18 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:44, 3 May 2008
Haemophilus influenzae 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
2A8C is a Single protein structure of sequence from Haemophilus influenzae. 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 Page seeded by OCA on Sat May 3 18:44:18 2008