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| | ==Crystal structure of pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase== | | ==Crystal structure of pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase== |
| - | <StructureSection load='1zco' size='340' side='right' caption='[[1zco]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='1zco' size='340' side='right'caption='[[1zco]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZCO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZCO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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]] 2.25Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-deoxy-7-phosphoheptulonate_synthase 3-deoxy-7-phosphoheptulonate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.54 2.5.1.54] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene></td></tr> |
| - | <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=1zco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zco OCA], [http://pdbe.org/1zco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zco RCSB], [http://www.ebi.ac.uk/pdbsum/1zco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zco 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=1zco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zco OCA], [https://pdbe.org/1zco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zco RCSB], [https://www.ebi.ac.uk/pdbsum/1zco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zco ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8U0A9_PYRFU Q8U0A9_PYRFU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1zco" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1zco" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[DAHP synthase 3D structures|DAHP synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-deoxy-7-phosphoheptulonate synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Atcc 43587]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Anderson, B F]] | + | [[Category: Anderson BF]] |
| - | [[Category: Jameson, G B]] | + | [[Category: Jameson GB]] |
| - | [[Category: Norris, G E]] | + | [[Category: Norris GE]] |
| - | [[Category: Parker, E J]] | + | [[Category: Parker EJ]] |
| - | [[Category: Patchett, M L]] | + | [[Category: Patchett ML]] |
| - | [[Category: Schofield, L R]] | + | [[Category: Schofield LR]] |
| - | [[Category: Arabino-heptulosonate]]
| + | |
| - | [[Category: Dah7p]]
| + | |
| - | [[Category: Dahp]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Shikimate]]
| + | |
| - | [[Category: Synthase]]
| + | |
| Structural highlights
Function
Q8U0A9_PYRFU
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
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAH7PS) catalyzes the condensation reaction between phosphoenolpyruvate (PEP) and the four-carbon monosaccharide D-erythrose 4-phosphate (E4P). DAH7PS from the hyperthermophile Pyrococcus furiosus is a member of the DAH7PS Ibeta subfamily, which also includes the KDO8PS enzymes. KDO8PS (3-deoxy-D-manno-octulosonate-8-phosphate synthase) catalyzes a closely related reaction of PEP with the five-carbon monosaccharide D-arabinose 5-phosphate (A5P). DAH7PS from P. furiosus requires a metal ion for activity and, unlike other characterized DAH7PS enzymes, is not inhibited by aromatic amino acids. Purified P. furiosus DAH7PS is able to utilize not only the four-carbon phosphorylated monosaccharides E4P and 2-deoxy-D-erythrose 4-phosphate but also the five-carbon phosphorylated monosaccharides A5P, D-ribose 5-phosphate, and 2-deoxy-D-ribose 5-phosphate with similar kcat but much increased KM values. DL-glyceraldehyde 3-phosphate and D-glucose 6-phosphate are not substrates. The structure of recombinant P. furiosus DAH7PS in complex with PEP was determined to 2.25 A resolution. The asymmetric unit consists of a dimer of (beta/alpha)8-barrel subunits. Analysis of the buried surfaces formed by dimerization and tetramerization, as observed in the crystal structure, provides insight into both the oligomeric status in solution and the substrate ambiguity of P. furiosus DAH7PS. P. furiosus DAH7PS is both the first archaeal and the first "naked" DAH7PS (without N-terminal extensions) to be fully characterized functionally and structurally. The broad substrate specificity of this DAH7PS, the lack of allosteric inhibition, and various structural features indicate that, of the enzymes characterized to date, P. furiosus DAH7PS may be the contemporary protein closest to the ancestral type I enzyme.
Substrate ambiguity and crystal structure of Pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase: an ancestral 3-deoxyald-2-ulosonate-phosphate synthase?,Schofield LR, Anderson BF, Patchett ML, Norris GE, Jameson GB, Parker EJ Biochemistry. 2005 Sep 13;44(36):11950-62. PMID:16142893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schofield LR, Anderson BF, Patchett ML, Norris GE, Jameson GB, Parker EJ. Substrate ambiguity and crystal structure of Pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase: an ancestral 3-deoxyald-2-ulosonate-phosphate synthase? Biochemistry. 2005 Sep 13;44(36):11950-62. PMID:16142893 doi:10.1021/bi050577z
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