1i6p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1i6p.jpg|left|200px]]
{{Seed}}
[[Image:1i6p.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i6p|  PDB=1i6p  |  SCENE=  }}  
{{STRUCTURE_1i6p|  PDB=1i6p  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_11316870}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11316870 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11316870}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Ph-dependent activity]]
[[Category: Ph-dependent activity]]
[[Category: Zinc coordination]]
[[Category: Zinc coordination]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:38:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:29:44 2008''

Revision as of 07:29, 1 July 2008

File:1i6p.png

Template:STRUCTURE 1i6p

CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)

Template:ABSTRACT PUBMED 11316870

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 Tue Jul 1 10:29:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1i6p&oldid=610418"