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6qhn
From Proteopedia
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<StructureSection load='6qhn' size='340' side='right'caption='[[6qhn]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6qhn' size='340' side='right'caption='[[6qhn]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6qhn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[6qhn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alphaproteobacteria Alphaproteobacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QHN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6qhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qhn OCA], [https://pdbe.org/6qhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qhn RCSB], [https://www.ebi.ac.uk/pdbsum/6qhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qhn 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=6qhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qhn OCA], [https://pdbe.org/6qhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qhn RCSB], [https://www.ebi.ac.uk/pdbsum/6qhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qhn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Salicylaldehyde dehydrogenase (SALD) catalyses the last reaction in the upper pathway of naphthalene degradation: the oxidation of salicylaldehyde to salicylate. This enzyme has been isolated and studied from a few organisms that belong to the betaproteobacteria and gammaproteobacteria, predominantly Pseudomonas putida. Furthermore, there is only one crystal structure of this enzyme, which was obtained from P. putida G7. Here, crystallographic studies and analysis of the crystal structure of an Alpine soil metagenome-derived SALD (SALDAP) from an alphaproteobacterium are presented. The SALDAP gene was discovered using gene-targeted sequence assembly and it was cloned into a pLATE51 vector. The recombinant protein was overexpressed in Escherichia coli BL21 (DE3) cells and the soluble protein was purified to homogeneity. The protein crystallized at 20 degrees C and diffraction data from the crystals were collected at a resolution of 1.9 A. The crystal belonged to the orthorhombic space group C2221, with unit-cell parameters a = 116.8, b = 121.7, c = 318.0 A. Analysis of the crystal structure revealed its conformation to be similar to the organization of the aldehyde dehydrogenase superfamily with three domains: the catalytic, NAD(+)-binding and bridging domains. The crystal structure of NahF from P. putida G7 was found to be the best structural homologue of SALDAP, even though the enzymes share only 48% amino-acid identity. Interestingly, a carboxylic acid (protocatechuic acid) was found to be a putative ligand of the enzyme and differential scanning fluorimetry was employed to confirm ligand binding. These findings open up the possibility of studying the mechanism(s) of product inhibition and biocatalysis of carboxylic acids using this enzyme and other related aldehyde dehydrogenases. | ||
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| + | Expression, purification and crystallization of a novel metagenome-derived salicylaldehyde dehydrogenase from Alpine soil.,Dandare SU, Hakansson M, Svensson LA, Timson DJ, Allen CCR Acta Crystallogr F Struct Biol Commun. 2022 Apr 1;78(Pt 4):161-169. doi:, 10.1107/S2053230X22002345. Epub 2022 Mar 28. PMID:35400668<ref>PMID:35400668</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6qhn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Alphaproteobacteria]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Allen | + | [[Category: Allen CCR]] |
| - | [[Category: Hakansson | + | [[Category: Hakansson M]] |
| - | [[Category: Shamsudeen | + | [[Category: Shamsudeen DU]] |
| - | [[Category: Svensson | + | [[Category: Svensson LA]] |
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Current revision
Metagenome-derived salicylaldehyde dehydrogenase from alpine soil in complex with protocatechuic acid
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