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| | <StructureSection load='2zvi' size='340' side='right'caption='[[2zvi]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2zvi' size='340' side='right'caption='[[2zvi]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zvi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZVI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zvi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZVI FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvi OCA], [http://pdbe.org/2zvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zvi RCSB], [http://www.ebi.ac.uk/pdbsum/2zvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvi ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvi OCA], [https://pdbe.org/2zvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvi RCSB], [https://www.ebi.ac.uk/pdbsum/2zvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MTNW_BACSU MTNW_BACSU]] Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).<ref>PMID:14551435</ref> | + | [https://www.uniprot.org/uniprot/MTNW_BACSU MTNW_BACSU] Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).<ref>PMID:14551435</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Inoue, T]] | + | [[Category: Inoue T]] |
| - | [[Category: Kai, Y]] | + | [[Category: Kai Y]] |
| - | [[Category: Matsumura, H]] | + | [[Category: Matsumura H]] |
| - | [[Category: Tamura, H]] | + | [[Category: Tamura H]] |
| - | [[Category: Yadani, T]] | + | [[Category: Yadani T]] |
| - | [[Category: Amino-acid biosynthesis]]
| + | |
| - | [[Category: Enolase]]
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| - | [[Category: Isomerase]]
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| - | [[Category: Magnesium]]
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| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Methionine biosynthesis]]
| + | |
| - | [[Category: Methionine salvage pathway]]
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| Structural highlights
Function
MTNW_BACSU Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).[1]
Publication Abstract from PubMed
2,3-Diketo-5-methylthiopentyl-1-phosphate enolase (DK-MTP-1P enolase), a RuBisCO-like protein (RLP), catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate. The crystal structure of the apo decarbamylated form (E form) of Bacillus subtilis DK-MTP-1P enolase (Bs-DK-MTP-1P enolase) has been determined at 2.3 A resolution. The overall structure of the E form of Bs-DK-MTP-1P enolase highly resembles that of Geobacillus kaustophilus DK-MTP-1P enolase (Gk-DK-MTP-1P enolase), with the exception of a few insertions or deletions and of a few residues at the active site. In the E form of Bs-DK-MTP-1P enolase, Lys150 (equivalent to Lys175 in RuBisCO) at the active site adopts a conformation that is distinct from those observed in the other forms of Gk-DK-MTP-1P enolase. This unusual conformational change appears to be induced by changes in the varphi and psi angles of Gly151, which is conserved in the sequences of the Bs-DK-MTP-1P and Gk-DK-MTP-1P enolases but not in those of RuBisCOs. The loop at 303-312, equivalent to the catalytic loop termed ;loop-6' in RuBisCO, is in a closed conformation in the E form of Bs-DK-MTP-1P enolase. The closed conformation appears to be stabilized by Pro312, which is conserved in the sequences of several RLPs (equivalent to Glu338 in RuBisCO). Based on these results, the characteristic structural features of DK-MTP-1P enolase are discussed.
Structure of the apo decarbamylated form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis.,Tamura H, Saito Y, Ashida H, Kai Y, Inoue T, Yokota A, Matsumura H Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):942-51. Epub 2009, Aug 14. PMID:19690372[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ashida H, Saito Y, Kojima C, Kobayashi K, Ogasawara N, Yokota A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science. 2003 Oct 10;302(5643):286-90. PMID:14551435 doi:10.1126/science.1086997
- ↑ Tamura H, Saito Y, Ashida H, Kai Y, Inoue T, Yokota A, Matsumura H. Structure of the apo decarbamylated form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis. Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):942-51. Epub 2009, Aug 14. PMID:19690372 doi:10.1107/S0907444909022422
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