From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1g9t.jpg|left|200px]] | + | {{Seed}} |
| + | [[Image:1g9t.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1g9t| PDB=1g9t | SCENE= }} | | {{STRUCTURE_1g9t| PDB=1g9t | SCENE= }} |
| | | |
- | '''CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX'''
| + | ===CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX=== |
| | | |
| | | |
- | ==Overview==
| + | <!-- |
- | Crystal structures have been determined for free Escherichia coli hypoxanthine phosphoribosyltransferase (HPRT) (2.9 A resolution) and for the enzyme in complex with the reaction products, inosine 5'-monophosphate (IMP) and guanosine 5'-monophosphate (GMP) (2.8 A resolution). Of the known 6-oxopurine phosphoribosyltransferase (PRTase) structures, E. coli HPRT is most similar in structure to that of Tritrichomonas foetus HGXPRT, with a rmsd for 150 Calpha atoms of 1.0 A. Comparison of the free and product bound structures shows that the side chain of Phe156 and the polypeptide backbone in this vicinity move to bind IMP or GMP. A nonproline cis peptide bond, also found in some other 6-oxopurine PRTases, is observed between Leu46 and Arg47 in both the free and complexed structures. For catalysis to occur, the 6-oxopurine PRTases have a requirement for divalent metal ion, usually Mg(2+) in vivo. In the free structure, a Mg(2+) is coordinated to the side chains of Glu103 and Asp104. This interaction may be important for stabilization of the enzyme before catalysis. E. coli HPRT is unique among the known 6-oxopurine PRTases in that it exhibits a marked preference for hypoxanthine as substrate over both xanthine and guanine. The structures suggest that its substrate specificity is due to the modes of binding of the bases. In E. coli HPRT, the carbonyl oxygen of Asp163 would likely form a hydrogen bond with the 2-exocyclic nitrogen of guanine (in the HPRT-guanine-PRib-PP-Mg(2+) complex). However, hypoxanthine does not have a 2-exocyclic atom and the HPRT-IMP structure suggests that hypoxanthine is likely to occupy a different position in the purine-binding pocket.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12070315}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12070315 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_12070315}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 33: |
Line 37: |
| [[Category: Protein chemistry]] | | [[Category: Protein chemistry]] |
| [[Category: Purine salvage]] | | [[Category: Purine salvage]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:19:36 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:57:45 2008'' |
Revision as of 01:57, 1 July 2008
Template:STRUCTURE 1g9t
CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX
Template:ABSTRACT PUBMED 12070315
About this Structure
1G9T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase., Guddat LW, Vos S, Martin JL, Keough DT, de Jersey J, Protein Sci. 2002 Jul;11(7):1626-38. PMID:12070315
Page seeded by OCA on Tue Jul 1 04:57:45 2008