2p4t: Difference between revisions
New page: left|200px<br /><applet load="2p4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p4t, resolution 1.15Å" /> '''Structure of the Q67... |
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[[Image:2p4t.jpg|left|200px]]<br /><applet load="2p4t" size=" | [[Image:2p4t.jpg|left|200px]]<br /><applet load="2p4t" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2p4t, resolution 1.15Å" /> | caption="2p4t, resolution 1.15Å" /> | ||
'''Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode'''<br /> | '''Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2P4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http:// | 2P4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4T OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: trimethoprim-resistance]] | [[Category: trimethoprim-resistance]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:01:31 2008'' | ||
Revision as of 16:01, 23 January 2008
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Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode
OverviewOverview
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 A, 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.
About this StructureAbout this Structure
2P4T is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Dihydrofolate reductase, with EC number 1.5.1.3 Full crystallographic information is available from OCA.
ReferenceReference
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
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