2ax2
From Proteopedia
(New page: 200px<br /> <applet load="2ax2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ax2, resolution 1.50Å" /> '''Production and X-ra...) |
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caption="2ax2, resolution 1.50Å" /> | caption="2ax2, resolution 1.50Å" /> | ||
'''Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II'''<br /> | '''Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human carbonic anhydrase II (HCA II) is a zinc metalloenzyme that | + | Human carbonic anhydrase II (HCA II) is a zinc metalloenzyme that catalyzes the reversible hydration and dehydration of carbon dioxide and bicarbonate, respectively. The rate-limiting step in catalysis is the intramolecular transfer of a proton between the zinc-bound solvent (H2O/OH-) and the proton-shuttling residue His64. This distance (approximately 7.5 A) is spanned by a well defined active-site solvent network stabilized by amino-acid side chains (Tyr7, Asn62, Asn67, Thr199 and Thr200). Despite the availability of high-resolution (approximately 1.0 A) X-ray crystal structures of HCA II, there is currently no definitive information available on the positions and orientations of the H atoms of the solvent network or active-site amino acids and their ionization states. In preparation for neutron diffraction studies to elucidate this hydrogen-bonding network, perdeuterated HCA II has been expressed, purified, crystallized and its X-ray structure determined to 1.5 A resolution. The refined structure is highly isomorphous with hydrogenated HCA II, especially with regard to the active-site architecture and solvent network. This work demonstrates the suitability of these crystals for neutron macromolecular crystallography. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AX2 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 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:// | + | 2AX2 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> 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=2AX2 OCA]. |
==Reference== | ==Reference== | ||
| - | Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II., Budayova-Spano M, Fisher SZ, Dauvergne MT, Agbandje-McKenna M, Silverman DN, Myles DA, McKenna R, Acta | + | Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II., Budayova-Spano M, Fisher SZ, Dauvergne MT, Agbandje-McKenna M, Silverman DN, Myles DA, McKenna R, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt 1):6-9., Epub 2005 Dec 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511248 16511248] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Budayova-Spano, M.]] | [[Category: Budayova-Spano, M.]] | ||
| - | [[Category: Dauvergne, M | + | [[Category: Dauvergne, M T.]] |
| - | [[Category: Fisher, S | + | [[Category: Fisher, S Z.]] |
| - | [[Category: McKenna, R | + | [[Category: McKenna, R M.]] |
| - | [[Category: Myles, D | + | [[Category: Myles, D A.A.]] |
| - | [[Category: Silverman, D | + | [[Category: Silverman, D N.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: perdeurated human carbonic anhydrase ii proton transfer]] | [[Category: perdeurated human carbonic anhydrase ii proton transfer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:54 2008'' |
Revision as of 14:31, 21 February 2008
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Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II
Contents |
Overview
Human carbonic anhydrase II (HCA II) is a zinc metalloenzyme that catalyzes the reversible hydration and dehydration of carbon dioxide and bicarbonate, respectively. The rate-limiting step in catalysis is the intramolecular transfer of a proton between the zinc-bound solvent (H2O/OH-) and the proton-shuttling residue His64. This distance (approximately 7.5 A) is spanned by a well defined active-site solvent network stabilized by amino-acid side chains (Tyr7, Asn62, Asn67, Thr199 and Thr200). Despite the availability of high-resolution (approximately 1.0 A) X-ray crystal structures of HCA II, there is currently no definitive information available on the positions and orientations of the H atoms of the solvent network or active-site amino acids and their ionization states. In preparation for neutron diffraction studies to elucidate this hydrogen-bonding network, perdeuterated HCA II has been expressed, purified, crystallized and its X-ray structure determined to 1.5 A resolution. The refined structure is highly isomorphous with hydrogenated HCA II, especially with regard to the active-site architecture and solvent network. This work demonstrates the suitability of these crystals for neutron macromolecular crystallography.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
2AX2 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II., Budayova-Spano M, Fisher SZ, Dauvergne MT, Agbandje-McKenna M, Silverman DN, Myles DA, McKenna R, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt 1):6-9., Epub 2005 Dec 16. PMID:16511248
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