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| | <StructureSection load='2wqt' size='340' side='right'caption='[[2wqt]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2wqt' size='340' side='right'caption='[[2wqt]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wqt]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wqt]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sv6|1sv6]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-oxopent-4-enoate_hydratase 2-oxopent-4-enoate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.80 4.2.1.80] </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=2wqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqt OCA], [https://pdbe.org/2wqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wqt RCSB], [https://www.ebi.ac.uk/pdbsum/2wqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqt 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=2wqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqt OCA], [https://pdbe.org/2wqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wqt RCSB], [https://www.ebi.ac.uk/pdbsum/2wqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MHPD_ECOLI MHPD_ECOLI] Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.<ref>PMID:9492273</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: 2-oxopent-4-enoate hydratase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Montgomery, M G]] | + | [[Category: Montgomery MG]] |
| - | [[Category: Wood, S P]] | + | [[Category: Wood SP]] |
| - | [[Category: Aromatic hydrocarbons catabolism]]
| + | |
| - | [[Category: Dodecahedral form]]
| + | |
| - | [[Category: Hydratase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
MHPD_ECOLI Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.[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 pentameric Escherichia coli enzyme 2-hydroxypentadienoic acid hydratase assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. The particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3-fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20-fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage and thus are ideal sites for addition of affinity tags or other modifications. These particles offer a convenient model system for studying the assembly of large symmetrical structures and a novel protein nanoparticle for encapsulation and cargo delivery.
Assembly of a 20-nm protein cage by Escherichia coli 2-hydroxypentadienoic acid hydratase.,Montgomery MG, Coker AR, Taylor IA, Wood SP J Mol Biol. 2010 Mar 12;396(5):1379-91. Epub 2010 Jan 4. PMID:20053352[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pollard JR, Bugg TD. Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli. Eur J Biochem. 1998 Jan 15;251(1-2):98-106. PMID:9492273
- ↑ Montgomery MG, Coker AR, Taylor IA, Wood SP. Assembly of a 20-nm protein cage by Escherichia coli 2-hydroxypentadienoic acid hydratase. J Mol Biol. 2010 Mar 12;396(5):1379-91. Epub 2010 Jan 4. PMID:20053352 doi:10.1016/j.jmb.2009.12.056
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