3hgj: Difference between revisions

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<StructureSection load='3hgj' size='340' side='right'caption='[[3hgj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3hgj' size='340' side='right'caption='[[3hgj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hgj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51532 Atcc 51532]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HGJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hgj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_scotoductus Thermus scotoductus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HGJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HBA:P-HYDROXYBENZALDEHYDE'>HBA</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hf3|3hf3]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HBA:P-HYDROXYBENZALDEHYDE'>HBA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CrS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37636 ATCC 51532])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] </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=3hgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hgj OCA], [https://pdbe.org/3hgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hgj RCSB], [https://www.ebi.ac.uk/pdbsum/3hgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hgj 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=3hgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hgj OCA], [https://pdbe.org/3hgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hgj RCSB], [https://www.ebi.ac.uk/pdbsum/3hgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hgj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B0JDW3_THESC B0JDW3_THESC]
== 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=3hgj 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=3hgj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recent characterization of the chromate reductase (CrS) from the thermophile Thermus scotoductus SA-01 revealed this enzyme to be related to the Old Yellow Enzyme (OYE) family. Here, we report the structure of a thermostable OYE homolog in its holoform at 2.2A as well as its complex with p-hydroxybenzaldehyde (pHBA). The enzyme crystallized as octamers with the monomers showing a classical TIM barrel fold which upon dimerization yields the biologically active form of the protein. A sulfate ion is bound above the si-side of the non-covalently bound FMN cofactor in the oxidized solved structure but is displaced upon pHBA binding. The active-site architecture is highly conserved as with other members of this enzyme family. The pHBA in the CrS complex is positioned by hydrogen bonding to the two conserved catalytic-site histidines. The most prominent structural difference between CrS and other OYE homologs is the size of the "capping domain". Thermostabilization of the enzyme is achieved in part through increased proline content within loops and turns as well as increased intersubunit interactions through hydrogen bonding and complex salt bridge networks. CrS is able to reduce the C=C bonds of alpha,beta-unsaturated carbonyl compounds with a preference towards cyclic substrates however no activity was observed towards beta-substituted substrates. Mutational studies have confirmed the role of Tyr177 as the proposed proton donor although reduction could still occur at a reduced rate when this residue was mutated to phenylalanine.
Crystal structure of a thermostable old yellow enzyme from Thermus scotoductus SA-01.,Opperman DJ, Sewell BT, Litthauer D, Isupov MN, Littlechild JA, van Heerden E Biochem Biophys Res Commun. 2010 Mar 12;393(3):426-31. Epub 2010 Feb 6. PMID:20138824<ref>PMID:20138824</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hgj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[NADPH dehydrogenase|NADPH dehydrogenase]]
*[[NADPH dehydrogenase|NADPH dehydrogenase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 51532]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: NADPH dehydrogenase]]
[[Category: Thermus scotoductus]]
[[Category: Heerden, E van]]
[[Category: Isupov MN]]
[[Category: Isupov, M N]]
[[Category: Litthauer D]]
[[Category: Litthauer, D]]
[[Category: Littlechild JA]]
[[Category: Littlechild, J A]]
[[Category: Opperman DJ]]
[[Category: Opperman, D J]]
[[Category: Sewell BT]]
[[Category: Sewell, B T]]
[[Category: Van Heerden E]]
[[Category: Oxidoreductase]]
[[Category: Tim barrel]]

Latest revision as of 11:27, 20 March 2024

Old Yellow Enzyme from Thermus scotoductus SA-01 complexed with p-hydroxy-benzaldehydeOld Yellow Enzyme from Thermus scotoductus SA-01 complexed with p-hydroxy-benzaldehyde

Structural highlights

3hgj is a 4 chain structure with sequence from Thermus scotoductus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B0JDW3_THESC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3hgj, resolution 2.00Å

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OCA
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