1vif

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[[Image:1vif.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE OF DIHYDROFOLATE REDUCTASE==
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|PDB= 1vif |SIZE=350|CAPTION= <scene name='initialview01'>1vif</scene>, resolution 1.8&Aring;
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<StructureSection load='1vif' size='340' side='right'caption='[[1vif]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>
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<table><tr><td colspan='2'>[[1vif]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIF FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE= SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vif OCA], [https://pdbe.org/1vif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vif RCSB], [https://www.ebi.ac.uk/pdbsum/1vif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vif ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vif OCA], [http://www.ebi.ac.uk/pdbsum/1vif PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vif RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DYR21_ECOLX DYR21_ECOLX] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR) exhibit high-level resistance to the antibiotic trimethoprim. Native R67 DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an inactive dimeric form. The structure of native R67 DHFR has now been solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR. Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing through the middle of the molecule. Two folate molecules bind asymmetrically within the pore indicating that the enzyme's active site consists of symmetry related binding surfaces from all four identical units.
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'''STRUCTURE OF DIHYDROFOLATE REDUCTASE'''
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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:7583655<ref>PMID:7583655</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1vif" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR) exhibit high-level resistance to the antibiotic trimethoprim. Native R67 DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an inactive dimeric form. The structure of native R67 DHFR has now been solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR. Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing through the middle of the molecule. Two folate molecules bind asymmetrically within the pore indicating that the enzyme's active site consists of symmetry related binding surfaces from all four identical units.
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*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1VIF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIF OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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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[[Category: Dihydrofolate reductase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Howell, E E.]]
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[[Category: Howell EE]]
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[[Category: Matthews, D A.]]
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[[Category: Matthews DA]]
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[[Category: Narayana, N.]]
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[[Category: Narayana N]]
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[[Category: Xuong, N H.]]
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[[Category: Xuong N-H]]
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[[Category: nadp]]
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[[Category: one-carbon metabolism]]
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[[Category: oxidoreductase]]
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[[Category: plasmid]]
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[[Category: trimethoprim resistance methotrexate resistance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:56 2008''
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Current revision

STRUCTURE OF DIHYDROFOLATE REDUCTASE

PDB ID 1vif

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