1doe
From Proteopedia
(Difference between revisions)
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<StructureSection load='1doe' size='340' side='right'caption='[[1doe]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1doe' size='340' side='right'caption='[[1doe]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1doe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1doe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DOB:2,4-DIHYDROXYBENZOIC+ACID'>DOB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DOB:2,4-DIHYDROXYBENZOIC+ACID'>DOB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1doe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doe OCA], [https://pdbe.org/1doe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1doe RCSB], [https://www.ebi.ac.uk/pdbsum/1doe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1doe 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=1doe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doe OCA], [https://pdbe.org/1doe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1doe RCSB], [https://www.ebi.ac.uk/pdbsum/1doe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1doe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHHY_PSEAE PHHY_PSEAE] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1doe ConSurf]. | </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=1doe ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis. | ||
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| - | The mobile flavin of 4-OH benzoate hydroxylase.,Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML Science. 1994 Oct 7;266(5182):110-4. PMID:7939628<ref>PMID:7939628</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1doe" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ballou | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Entsch | + | [[Category: Ballou DP]] |
| - | [[Category: Gatti | + | [[Category: Entsch B]] |
| - | [[Category: Lah | + | [[Category: Gatti DL]] |
| - | [[Category: Ludwig | + | [[Category: Lah MS]] |
| - | [[Category: Massey | + | [[Category: Ludwig ML]] |
| - | [[Category: Palfey | + | [[Category: Massey V]] |
| - | + | [[Category: Palfey BA]] | |
Current revision
THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS
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