3chh
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3chh.png|left|200px]] | ||
| - | + | ==Crystal Structure of Di-iron AurF== | |
| - | + | <StructureSection load='3chh' size='340' side='right'caption='[[3chh]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3chh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_thioluteus Streptomyces thioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHH FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></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=3chh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chh OCA], [https://pdbe.org/3chh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chh RCSB], [https://www.ebi.ac.uk/pdbsum/3chh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chh ProSAT]</span></td></tr> |
| - | [[3chh]] is a 2 chain structure with sequence from [ | + | </table> |
| - | + | == Function == | |
| - | == | + | [https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:20798054, PubMed:18458342). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref> |
| - | < | + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chh_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3chh ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Streptomyces thioluteus]] | [[Category: Streptomyces thioluteus]] | ||
| - | [[Category: Brunzelle | + | [[Category: Brunzelle JS]] |
| - | [[Category: Nair | + | [[Category: Nair SK]] |
| - | [[Category: Zhang | + | [[Category: Zhang H]] |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Di-iron AurF
| |||||||||||
