2fgc: Difference between revisions
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==Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritima== | ==Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritima== | ||
<StructureSection load='2fgc' size='340' side='right' caption='[[2fgc]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2fgc' size='340' side='right'caption='[[2fgc]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fgc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FGC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2fgc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FGC FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acetolactate synthase]] | [[Category: Acetolactate synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: Thema]] | [[Category: Thema]] | ||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
Revision as of 13:49, 18 March 2020
Crystal structure of Acetolactate synthase- small subunit from Thermotoga maritimaCrystal structure of Acetolactate synthase- small subunit from Thermotoga maritima
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 PubMedCrystal structures of two orthologs of the regulatory subunit of acetohydroxyacid synthase III (AHAS, EC 2.2.1.6) from Thermotoga maritima (TM0549) and Nitrosomonas europea (NE1324) were determined by single-wavelength anomalous diffraction methods with the use of selenomethionine derivatives at 2.3 A and 2.5 A, respectively. TM0549 and NE1324 share the same fold, and in both proteins the polypeptide chain contains two separate domains of a similar size. Each protein contains a C-terminal domain with ferredoxin-type fold and an N-terminal ACT domain, of which the latter is characteristic for several proteins involved in amino acid metabolism. The ferredoxin domain is stabilized by a calcium ion in the crystal structure of NE1324 and by a Mg(H2O)(6)2+ ion in TM0549. Both TM0549 and NE1324 form dimeric assemblies in the crystal lattice. Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit.,Petkowski JJ, Chruszcz M, Zimmerman MD, Zheng H, Skarina T, Onopriyenko O, Cymborowski MT, Koclega KD, Savchenko A, Edwards A, Minor W Protein Sci. 2007 Jul;16(7):1360-7. PMID:17586771[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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