3acd

Crystal structure of hypoxanthine-guanine phosphoribosyltransferase with IMP from Thermus thermophilus HB8

spinqualitylabelsall models 3acd, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3acd is a 1 chain structure with sequence from Thermus thermophilus HB8. This structure supersedes the now removed PDB entry 2ywu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.89Å Ligands: DIO, IMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SLS3_THET8 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hypoxanthine-guanine phosphoribosyltransferase (HGPRTase), which is a key enzyme in the purine-salvage pathway, catalyzes the synthesis of IMP or GMP from alpha-D-phosphoribosyl-1-pyrophosphate and hypoxanthine or guanine, respectively. Structures of HGPRTase from Thermus thermophilus HB8 in the unliganded form, in complex with IMP and in complex with GMP have been determined at 2.1, 1.9 and 2.2 A resolution, respectively. The overall fold of the IMP complex was similar to that of the unliganded form, but the main-chain and side-chain atoms of the active site moved to accommodate IMP. The overall folds of the IMP and GMP complexes were almost identical to each other. Structural comparison of the T. thermophilus HB8 enzyme with 6-oxopurine PRTases for which structures have been determined showed that these enzymes can be tentatively divided into groups I and II and that the T. thermophilus HB8 enzyme belongs to group I. The group II enzymes are characterized by an N-terminal extension with additional secondary elements and a long loop connecting the second alpha-helix and beta-strand compared with the group I enzymes. Structures of hypoxanthine-guanine phosphoribosyltransferase (TTHA0220) from Thermus thermophilus HB8.,Kanagawa M, Baba S, Ebihara A, Shinkai A, Hirotsu K, Mega R, Kim K, Kuramitsu S, Sampei G, Kawai G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):893-8. Epub 2010 Jul 27. PMID:20693661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoribosyltransferase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA