1o5q
From Proteopedia
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|PDB= 1o5q |SIZE=350|CAPTION= <scene name='initialview01'>1o5q</scene>, resolution 2.30Å | |PDB= 1o5q |SIZE=350|CAPTION= <scene name='initialview01'>1o5q</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] </span> |
|GENE= prpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium]) | |GENE= prpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ujq|1UJQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o5q OCA], [http://www.ebi.ac.uk/pdbsum/1o5q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o5q RCSB]</span> | ||
}} | }} | ||
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[[Category: Murthy, M R.N.]] | [[Category: Murthy, M R.N.]] | ||
[[Category: Simanshu, D K.]] | [[Category: Simanshu, D K.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PYR]] | ||
[[Category: helix swapping]] | [[Category: helix swapping]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
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[[Category: prpb]] | [[Category: prpb]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:13 2008'' |
Revision as of 19:40, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | prpB (Salmonella enterica subsp. enterica serovar Typhimurium) | ||||||
| Activity: | Methylisocitrate lyase, with EC number 4.1.3.30 | ||||||
| Related: | 1UJQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pyruvate and Mg2+ bound 2-methylisocitrate lyase (PrpB) from Salmonella typhimurium
Overview
Propionate metabolism in Salmonella typhimurium occurs via 2-methylcitric acid cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate, is catalysed by 2-methylisocitrate lyase (PrpB). Here we report the X-ray crystal structure of the native and the pyruvate/Mg(2+) bound PrpB from S. typhimurium, determined at 2.1 and 2.3A, respectively. The structure closely resembles that of the Escherichia coli enzyme. Unlike the E. coli PrpB, Mg(2+) could not be located in the native Salmonella PrpB. Only in pyruvate bound PrpB structure, Mg(2+) was found coordinated with pyruvate. Binding of pyruvate to PrpB seems to induce movement of the Mg(2+) by 2.5A from its position found in E. coli native PrpB. In both the native enzyme and pyruvate/Mg(2+) bound forms, the active site loop is completely disordered. Examination of the pocket in which pyruvate and glyoxalate bind to 2-methylisocitrate lyase and isocitrate lyase, respectively, reveals plausible rationale for different substrate specificities of these two enzymes. Structural similarities in substrate and metal atom binding site as well as presence of similar residues in the active site suggest possible similarities in the reaction mechanism.
About this Structure
1O5Q is a Single protein structure of sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA.
Reference
Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+)., Simanshu DK, Satheshkumar PS, Savithri HS, Murthy MR, Biochem Biophys Res Commun. 2003 Nov 7;311(1):193-201. PMID:14575713
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