5zyr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the reductase (C1) component of p-hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii== | |
| + | <StructureSection load='5zyr' size='340' side='right'caption='[[5zyr]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zyr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin_reductase_(NADH) Flavin reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.36 1.5.1.36] </span></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=5zyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyr OCA], [http://pdbe.org/5zyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyr RCSB], [http://www.ebi.ac.uk/pdbsum/5zyr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HPAHR_ACIBA HPAHR_ACIBA]] Reductase component of a two-component system that supplies reduced FMN (FMNH2) to the oxygenase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the oxygenase component C2.<ref>PMID:11683878</ref> <ref>PMID:16042421</ref> <ref>PMID:17595116</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | p-Hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii catalyzes the hydroxylation of p-hydroxyphenylacetate (HPA) at the ortho position to yield 3,4-dihydroxyphenylacetate (DHPA). HPAH from A. baumannii is a two-component flavoprotein consisting of a smaller reductase (C(1)) component and a larger oxygenase (C(2)) component. The C(1) component supplies a reduced flavin in its free form to the C(2) counterpart for hydroxylation. In addition, HPA can bind to C(1) and enhance the flavin-reduction rate without becoming hydroxylated. The recombinant C(1) component was purified and crystallized using the microbatch method at 295 K. X-ray diffraction data were collected to 2.3 A resolution using synchrotron radiation on the BL13B1 beamline at NSRRC, Taiwan. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.78, b = 59.92, c = 211.85 A, and contained two molecules of C(1) per asymmetric unit. | ||
| - | + | Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii.,Oonanant W, Sucharitakul J, Chaiyen P, Yuvaniyama J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):720-3. doi:, 10.1107/S1744309112016909. Epub 2012 May 24. PMID:22684080<ref>PMID:22684080</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5zyr" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Chaiyen, P]] | [[Category: Chaiyen, P]] | ||
| - | [[Category: Sucharitakul, J]] | ||
[[Category: Oonanant, W]] | [[Category: Oonanant, W]] | ||
| + | [[Category: Phongsak, T]] | ||
| + | [[Category: Sucharitakul, J]] | ||
| + | [[Category: Yuvaniyama, J]] | ||
| + | [[Category: Acinetobacter baumannii]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Monooxygenase]] | ||
| + | [[Category: Reductase]] | ||
Revision as of 22:40, 5 June 2019
Crystal structure of the reductase (C1) component of p-hydroxyphenylacetate 3-hydroxylase (HPAH) from Acinetobacter baumannii
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