1h5y: Difference between revisions
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==HisF protein from Pyrobaculum aerophilum== | ==HisF protein from Pyrobaculum aerophilum== | ||
<StructureSection load='1h5y' size='340' side='right' caption='[[1h5y]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1h5y' size='340' side='right'caption='[[1h5y]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h5y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[1h5y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5Y FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 51768]] | [[Category: Atcc 51768]] | ||
[[Category: Large Structures]] | |||
[[Category: Baker, E N]] | [[Category: Baker, E N]] | ||
[[Category: Banfield, M J]] | [[Category: Banfield, M J]] | ||
Revision as of 11:32, 23 October 2019
HisF protein from Pyrobaculum aerophilumHisF protein from Pyrobaculum aerophilum
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHisF (imidazole glycerol phosphate synthase) is an important branch-point enzyme in the histidine biosynthetic pathway of microorganisms. Because of its potential relevance for structure-based drug design, the crystal structure of HisF from the hyperthermophilic archaeon Pyrobaculum aerophilum has been determined. The structure was determined by molecular replacement and refined at 2.0 A resolution to a crystallographic R factor of 20.6% and a free R of 22.7%. The structure adopts a classic (beta/alpha)(8) barrel fold and has networks of surface salt bridges that may contribute to thermostability. The active site is marked out by the presence of two bound phosphate ions and two glycerol molecules that delineate a long groove at one end of the (beta/alpha)(8) barrel. The two phosphate ions, 17 A apart, are bound to sequence-conserved structural motifs that seem likely to provide much of the specificity for the two phosphate groups of the HisF substrate. The two glycerol molecules bind in the vicinity of other sequence-conserved residues that are likely to be involved in binding and/or catalysis. Comparisons with the homologous HisF from Thermatoga maritima reveal a displaced loop that may serve as a lid over the active site. Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum.,Banfield MJ, Lott JS, Arcus VL, McCarthy AA, Baker EN Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1518-25. Epub 2001, Oct 25. PMID:11679715[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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