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| | <StructureSection load='2yyk' size='340' side='right'caption='[[2yyk]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='2yyk' size='340' side='right'caption='[[2yyk]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YYK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yyg|2yyg]], [[2yyi|2yyi]], [[2yyj|2yyj]], [[2yyl|2yyl]], [[2yym|2yym]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-hydroxyphenylacetate_3-monooxygenase 4-hydroxyphenylacetate 3-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.9 1.14.14.9] </span></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=2yyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yyk OCA], [https://pdbe.org/2yyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yyk RCSB], [https://www.ebi.ac.uk/pdbsum/2yyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yyk ProSAT]</span></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=2yyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yyk OCA], [https://pdbe.org/2yyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yyk RCSB], [https://www.ebi.ac.uk/pdbsum/2yyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yyk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/HPAB_THET8 HPAB_THET8]] Utilizes FADH(2) supplied by HpaC, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).<ref>PMID:17804419</ref>
| + | [https://www.uniprot.org/uniprot/HPAB_THET8 HPAB_THET8] Utilizes FADH(2) supplied by HpaC, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).<ref>PMID:17804419</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxyphenylacetate 3-monooxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Ebihara, A]] | + | [[Category: Ebihara A]] |
| - | [[Category: Hisano, T]] | + | [[Category: Hisano T]] |
| - | [[Category: Iwasaki, W]] | + | [[Category: Iwasaki W]] |
| - | [[Category: Kim, S H]] | + | [[Category: Kim S-H]] |
| - | [[Category: Miki, K]] | + | [[Category: Miki K]] |
| - | [[Category: Takeda, K]] | + | [[Category: Takeda K]] |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygnase component]]
| + | |
| - | [[Category: Riken spring-8 center]]
| + | |
| - | [[Category: Structurome]]
| + | |
| - | [[Category: Two-component flavin diffusible monooxygenase]]
| + | |
| - | [[Category: Unligand form]]
| + | |
| Structural highlights
Function
HPAB_THET8 Utilizes FADH(2) supplied by HpaC, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).[1]
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 PubMed
The 4-hydroxyphenylacetate (4HPA) 3-monooxygenase is involved in the initial step of the 4HPA degradation pathway and catalyzes 4HPA hydroxylation to 3,4-dihydroxyphenylacetate. This enzyme consists of two components, an oxygenase (HpaB) and a reductase (HpaC). To understand the structural basis of the catalytic mechanism of HpaB, crystal structures of HpaB from Thermus thermophilus HB8 were determined in three states: a ligand-free form, a binary complex with FAD, and a ternary complex with FAD and 4HPA. Structural analysis revealed that the binding and dissociation of flavin are accompanied by conformational changes of the loop between beta5 and beta6 and of the loop between beta8 and beta9, leading to preformation of part of the substrate-binding site (Ser-197 and Thr-198). The latter loop further changes its conformation upon binding of 4HPA and obstructs the active site from the bulk solvent. Arg-100 is located adjacent to the putative oxygen-binding site and may be involved in the formation and stabilization of the C4a-hydroperoxyflavin intermediate.
Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8.,Kim SH, Hisano T, Takeda K, Iwasaki W, Ebihara A, Miki K J Biol Chem. 2007 Nov 9;282(45):33107-17. Epub 2007 Sep 5. PMID:17804419[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim SH, Hisano T, Takeda K, Iwasaki W, Ebihara A, Miki K. Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8. J Biol Chem. 2007 Nov 9;282(45):33107-17. Epub 2007 Sep 5. PMID:17804419 doi:10.1074/jbc.M703440200
- ↑ Kim SH, Hisano T, Takeda K, Iwasaki W, Ebihara A, Miki K. Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8. J Biol Chem. 2007 Nov 9;282(45):33107-17. Epub 2007 Sep 5. PMID:17804419 doi:10.1074/jbc.M703440200
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