2r5v

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<StructureSection load='2r5v' size='340' side='right' caption='[[2r5v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2r5v' size='340' side='right' caption='[[2r5v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2r5v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R5V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2r5v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_orientalis"_pittenger_and_brigham_1956 "streptomyces orientalis" pittenger and brigham 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R5V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HHH:(2S)-HYDROXY(4-HYDROXYPHENYL)ETHANOIC+ACID'>HHH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HHH:(2S)-HYDROXY(4-HYDROXYPHENYL)ETHANOIC+ACID'>HHH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HmaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31958 Amycolatopsis orientalis])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HmaS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31958 "Streptomyces orientalis" Pittenger and Brigham 1956])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxymandelate_synthase 4-hydroxymandelate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.46 1.13.11.46] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxymandelate_synthase 4-hydroxymandelate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.46 1.13.11.46] </span></td></tr>
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<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=2r5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r5v RCSB], [http://www.ebi.ac.uk/pdbsum/2r5v PDBsum]</span></td></tr>
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<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=2r5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5v OCA], [http://pdbe.org/2r5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r5v RCSB], [http://www.ebi.ac.uk/pdbsum/2r5v PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/O52791_AMYOR O52791_AMYOR]] Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.<ref>PMID:11137816</ref>
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[[http://www.uniprot.org/uniprot/HMAS_AMYOR HMAS_AMYOR]] Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.<ref>PMID:11137816</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2r5v" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Streptomyces orientalis pittenger and brigham 1956]]
[[Category: 4-hydroxymandelate synthase]]
[[Category: 4-hydroxymandelate synthase]]
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[[Category: Amycolatopsis orientalis]]
 
[[Category: Brownlee, J M]]
[[Category: Brownlee, J M]]
[[Category: Harrison, D H.T]]
[[Category: Harrison, D H.T]]

Revision as of 13:05, 10 September 2015

Hydroxymandelate Synthase Crystal Structure

2r5v, resolution 2.30Å

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