This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2ax2.gif|left|200px]]<br /> | + | [[Image:2ax2.gif|left|200px]]<br /><applet load="2ax2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ax2" size=" | + | |
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== | ||
| Line 11: | Line 10: | ||
==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
|
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
Page seeded by OCA on Thu Feb 21 16:31:54 2008
