1vie: Difference between revisions
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<StructureSection load='1vie' size='340' side='right'caption='[[1vie]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1vie' size='340' side='right'caption='[[1vie]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vie]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1vie]] 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=1VIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIE FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vie OCA], [https://pdbe.org/1vie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vie RCSB], [https://www.ebi.ac.uk/pdbsum/1vie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vie ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Howell | [[Category: Howell EE]] | ||
[[Category: Matthews | [[Category: Matthews DA]] | ||
[[Category: Narayana | [[Category: Narayana N]] | ||
[[Category: Xuong | [[Category: Xuong N-H]] | ||
Revision as of 07:05, 7 October 2022
STRUCTURE OF DIHYDROFOLATE REDUCTASESTRUCTURE OF DIHYDROFOLATE REDUCTASE
Structural highlights
FunctionDYR21_ECOLX Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Publication Abstract from PubMedBacteria 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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