2ax2

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2ax2, resolution 1.50Å

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Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II

OverviewOverview

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.

DiseaseDisease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this StructureAbout this Structure

2AX2 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

ReferenceReference

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 Crystallograph Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt, 1):6-9. Epub 2005 Dec 16. PMID:16511248

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