1h75: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h75]] is a 1 chain structure with 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=1H75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H75 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1h75]] is a 1 chain structure with 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=1H75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H75 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h75 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h75 RCSB], [http://www.ebi.ac.uk/pdbsum/1h75 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h75 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h75 RCSB], [http://www.ebi.ac.uk/pdbsum/1h75 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Aslund, F | [[Category: Aslund, F]] | ||
[[Category: Holmgren, A | [[Category: Holmgren, A]] | ||
[[Category: Lindqvist, Y | [[Category: Lindqvist, Y]] | ||
[[Category: Schneider, G | [[Category: Schneider, G]] | ||
[[Category: Stehr, M | [[Category: Stehr, M]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Glutaredoxin]] | [[Category: Glutaredoxin]] | ||
Revision as of 23:43, 22 December 2014
STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI.STRUCTURAL BASIS FOR THE THIOREDOXIN-LIKE ACTIVITY PROFILE OF THE GLUTAREDOXIN-LIKE PROTEIN NRDH-REDOXIN FROM ESCHERICHIA COLI.
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 PubMedNrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. The crystal structure of recombinant Escherichia coli NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the thioredoxin superfamily and is structurally most similar to E. coli glutaredoxin 3 and phage T4 glutaredoxin. The angle between the C-terminal helix alpha3 and strand beta4, which differs between thioredoxin and glutaredoxin, has an intermediate value in NrdH-redoxin. The orientation of this helix is to a large extent determined by an extended hydrogen-bond network involving the highly conserved sequence motif (61)WSGFRP(D/E)(67), which is unique to this subclass of the thioredoxin superfamily. Residues that bind glutathione in glutaredoxins are in general not conserved in NrdH-redoxin, and no glutathione-binding cleft is present. Instead, NrdH-redoxin contains a wide hydrophobic pocket at the surface, similar to thioredoxin. Modeling studies suggest that NrdH-redoxin can interact with E. coli thioredoxin reductase at this pocket and also via a loop that is complementary to a crevice in the reductase in a similar manner as observed in the E. coli thioredoxin-thioredoxin reductase complex. Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli.,Stehr M, Schneider G, Aslund F, Holmgren A, Lindqvist Y J Biol Chem. 2001 Sep 21;276(38):35836-41. Epub 2001 Jul 5. PMID:11441020[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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