1moo
From Proteopedia
(New page: 200px<br /> <applet load="1moo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1moo, resolution 1.05Å" /> '''Site Specific Mutan...) |
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| - | [[Image:1moo.gif|left|200px]]<br /> | + | [[Image:1moo.gif|left|200px]]<br /><applet load="1moo" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1moo" size=" | + | |
caption="1moo, resolution 1.05Å" /> | caption="1moo, resolution 1.05Å" /> | ||
'''Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution'''<br /> | '''Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Using synchrotron radiation and a CCD detector, X-ray data have been | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MOO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, HG and 4MZ as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1MOO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=4MZ:'>4MZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1MOO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Agbandje-McKenna, M.]] | [[Category: Agbandje-McKenna, M.]] | ||
| - | [[Category: Duda, D | + | [[Category: Duda, D M.]] |
[[Category: Govindasamy, L.]] | [[Category: Govindasamy, L.]] | ||
[[Category: McKenna, R.]] | [[Category: McKenna, R.]] | ||
| - | [[Category: Silverman, D | + | [[Category: Silverman, D N.]] |
| - | [[Category: Tu, C | + | [[Category: Tu, C K.]] |
[[Category: 4MZ]] | [[Category: 4MZ]] | ||
[[Category: HG]] | [[Category: HG]] | ||
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[[Category: zinc metalloenzyme]] | [[Category: zinc metalloenzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:22 2008'' |
Revision as of 11:57, 21 February 2008
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Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution
Contents |
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.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1MOO is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 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
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