3ACC
Crystal structure of hypoxanthine-guanine phosphoribosyltransferase with GMP from Thermus thermophilus HB8
Replaces: 2YWTSummary for 3ACC
| Entry DOI | 10.2210/pdb3acc/pdb |
| Related | 3ACB 3ACD |
| Descriptor | Hypoxanthine-guanine phosphoribosyltransferase, GUANOSINE-5'-MONOPHOSPHATE, 1,4-DIETHYLENE DIOXIDE, ... (4 entities in total) |
| Functional Keywords | rossmann fold, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transferase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 20732.69 |
| Authors | Kanagawa, M.,Baba, S.,Hirotsu, K.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.,Sampei, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-12-30, release date: 2010-02-09, Last modification date: 2023-11-01) |
| Primary citation | Kanagawa, M.,Baba, S.,Ebihara, A.,Shinkai, A.,Hirotsu, K.,Mega, R.,Kim, K.,Kuramitsu, S.,Sampei, G.,Kawai, G. Structures of hypoxanthine-guanine phosphoribosyltransferase (TTHA0220) from Thermus thermophilus HB8. Acta Crystallogr.,Sect.F, 66:893-898, 2010 Cited by PubMed Abstract: 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. PubMed: 20693661DOI: 10.1107/S1744309110023079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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