1i6p: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="1i6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6p, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1i6p.jpg|left|200px]]<br /><applet load="1i6p" size=" | [[Image:1i6p.jpg|left|200px]]<br /><applet load="1i6p" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1i6p, resolution 2.00Å" /> | caption="1i6p, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)'''<br /> | '''CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)'''<br /> | ||
==Overview== | ==Overview== | ||
Carbonic anhydrases fall into three distinct evolutionary and structural | 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== | ==About this Structure== | ||
1I6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http:// | 1I6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6P OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cronk, J | [[Category: Cronk, J D.]] | ||
[[Category: Cronk, M | [[Category: Cronk, M R.]] | ||
[[Category: Endrizzi, J | [[Category: Endrizzi, J A.]] | ||
[[Category: Neill, J | [[Category: Neill, J W.O.]] | ||
[[Category: Zhang, K | [[Category: Zhang, K Y.J.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: carbonic anhydrase]] | [[Category: carbonic anhydrase]] | ||
| Line 27: | Line 27: | ||
[[Category: zinc coordination]] | [[Category: zinc coordination]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:30 2008'' | ||
