1moo
From Proteopedia
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[[Image:1moo.gif|left|200px]] | [[Image:1moo.gif|left|200px]] | ||
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'''Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution''' | '''Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution''' | ||
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[[Category: Tu, C K.]] | [[Category: Tu, C K.]] | ||
[[Category: 4-methylimidazole]] | [[Category: 4-methylimidazole]] | ||
| - | [[Category: | + | [[Category: High-resolution]] |
| - | [[Category: | + | [[Category: Twisted beta sheet]] |
| - | [[Category: | + | [[Category: Zinc metalloenzyme]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:31:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:31, 2 May 2008
Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution
Overview
Using synchrotron radiation and a CCD detector, X-ray data have been collected at 100 K for the His64Ala mutant of human carbonic anhydrase II complexed with 4-methylimidazole (4-MI) to a maximal 1.05 A resolution, allowing full anisotropic least-squares refinement. The refined model has a conventional R factor of 15.7% for all reflections. The C(alpha) coordinates of the model presented here have an r.m.s. deviation of 0.10 A relative to the previously determined structure at 1.6 A resolution. Several amino-acid residues (six of the 255 observed) have been identified with multiple rotamer side-chain conformations. C, N and O atoms can be differentiated with selective electron-density map contouring. The estimated standard deviations for all main-chain non-H atom bond lengths and angles are 0.013 and 0.030 A, respectively, based on unrestrained full-matrix least-squares refinement. This structure gives detailed information about the tetrahedrally arranged zinc ion coordinated by three histidine N atoms (His94 N(epsilon 2), His96 N(epsilon2) and His119 N(delta1)) and a water/hydroxide, the multiple binding sites of the proton chemical rescue molecule 4-MI and the solvent networks linking the zinc-bound water/hydroxide and 4-MI molecules. This structure presents the highest resolution structure of a carbonic anhydrase isozyme so far determined and adds to the understanding of proton-transfer processes.
About this Structure
1MOO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer., Duda D, Govindasamy L, Agbandje-McKenna M, Tu C, Silverman DN, McKenna R, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):93-104. Epub 2002, Dec 19. PMID:12499545 Page seeded by OCA on Sat May 3 01:31:41 2008
