2p4t

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{{STRUCTURE_2p4t| PDB=2p4t | SCENE= }}
{{STRUCTURE_2p4t| PDB=2p4t | SCENE= }}
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'''Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode'''
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===Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode===
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==Overview==
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Plasmid-encoded bacterial R67 dihydrofolate reductase (DHFR) is a NADPH-dependent enzyme unrelated to chromosomal DHFR in amino acid sequence and structure. R67 DHFR is insensitive to the bacterial drug trimethoprim in contrast to chromosomal DHFR. The crystal structure of Q67H mutant of R67 DHFR bound to NADP(+) has been determined at 1.15 angstroms resolution. The cofactor assumes an extended conformation with the nicotinamide ring bound near the center of the active site pore, the ribose and pyrophosphate group (PP(i)) extending toward the outer pore. The ribonicotinamide exhibits anti conformation as in chromosomal DHFR complexes. The relative orientation between the PP(i) and the nicotinamide ribose differs from that observed in chromosomal DHFR-NADP(+) complexes. The coenzyme displays symmetrical binding mode with several water-mediated hydrogen bonds with the protein besides ionic, stacking, and van der Waals interactions. The structure provides a molecular basis for the observed stoichiometry and cooperativity in ligand binding. The ternary model based on the present structure and the previous R67 DHFR-folate complex provides insight into the catalytic mechanism and indicates that the relative orientation of the reactants in plasmid DHFR is different from that seen in chromosomal DHFRs.
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(as it appears on PubMed at http://www.pubmed.gov), where 17473013 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17473013}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode., Divya N, Grifith E, Narayana N, Protein Sci. 2007 Jun;16(6):1063-8. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473013 17473013]
Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode., Divya N, Grifith E, Narayana N, Protein Sci. 2007 Jun;16(6):1063-8. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473013 17473013]
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High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in the D2-symmetric active site., Narayana N, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):695-706. Epub 2006, Jun 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16790925 16790925]
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A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site., Narayana N, Matthews DA, Howell EE, Nguyen-huu X, Nat Struct Biol. 1995 Nov;2(11):1018-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7583655 7583655]
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A glutamine 67--&gt; histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition., Park H, Bradrick TD, Howell EE, Protein Eng. 1997 Dec;10(12):1415-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9543003 9543003]
[[Category: Dihydrofolate reductase]]
[[Category: Dihydrofolate reductase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Symmetric binding]]
[[Category: Symmetric binding]]
[[Category: Trimethoprim-resistance]]
[[Category: Trimethoprim-resistance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:21:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:31:20 2008''

Revision as of 23:31, 28 July 2008

Image:2p4t.png

Template:STRUCTURE 2p4t

Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode

Template:ABSTRACT PUBMED 17473013

About this Structure

2P4T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode., Divya N, Grifith E, Narayana N, Protein Sci. 2007 Jun;16(6):1063-8. Epub 2007 May 1. PMID:17473013

High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in the D2-symmetric active site., Narayana N, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):695-706. Epub 2006, Jun 20. PMID:16790925

A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site., Narayana N, Matthews DA, Howell EE, Nguyen-huu X, Nat Struct Biol. 1995 Nov;2(11):1018-25. PMID:7583655

A glutamine 67--> histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition., Park H, Bradrick TD, Howell EE, Protein Eng. 1997 Dec;10(12):1415-24. PMID:9543003

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