1usl
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert | + | Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the synthesis of ribose from other sugars, as well a means for salvage of carbohydrates after nucleotide breakdown. Two unrelated types of enzyme are known to catalyze the isomerization. The most common one, RpiA, is present in almost all organisms. The second type, RpiB, is found in many bacterial species.Here, we demonstrate that the RpiB from Mycobacterium tuberculosis (Rv2465c) has catalytic properties very similar to those previously reported for the Escherichia coli RpiB enzyme. Further, we report the structure of the mycobacterial enzyme, solved by molecular replacement and refined to 1.88A resolution. Comparison with the E.coli structure shows that there are important differences in the two active sites, including a change in the position and nature of the catalytic base. Sequence comparisons reveal that the M.tuberculosis and E.coli RpiB enzymes are in fact representative of two distinct sub-families. The mycobacterial enzyme represents a type found only in actinobacteria, while the enzyme from E.coli is typical of that seen in many other bacterial proteomes. Both RpiBs are very different from RpiA in structure as well as in the construction of the active site. Docking studies allow additional insights into the reactions of all three enzymes, and show that many features of the mechanism are preserved despite the different catalytic components. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Ribose-5-phosphate isomerase]] | [[Category: Ribose-5-phosphate isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Andersson, C | + | [[Category: Andersson, C E.]] |
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
| - | [[Category: Roos, A | + | [[Category: Roos, A K.]] |
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: Unge, T.]] | [[Category: Unge, T.]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:00 2008'' |
Revision as of 13:28, 21 February 2008
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STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE.
Overview
Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the synthesis of ribose from other sugars, as well a means for salvage of carbohydrates after nucleotide breakdown. Two unrelated types of enzyme are known to catalyze the isomerization. The most common one, RpiA, is present in almost all organisms. The second type, RpiB, is found in many bacterial species.Here, we demonstrate that the RpiB from Mycobacterium tuberculosis (Rv2465c) has catalytic properties very similar to those previously reported for the Escherichia coli RpiB enzyme. Further, we report the structure of the mycobacterial enzyme, solved by molecular replacement and refined to 1.88A resolution. Comparison with the E.coli structure shows that there are important differences in the two active sites, including a change in the position and nature of the catalytic base. Sequence comparisons reveal that the M.tuberculosis and E.coli RpiB enzymes are in fact representative of two distinct sub-families. The mycobacterial enzyme represents a type found only in actinobacteria, while the enzyme from E.coli is typical of that seen in many other bacterial proteomes. Both RpiBs are very different from RpiA in structure as well as in the construction of the active site. Docking studies allow additional insights into the reactions of all three enzymes, and show that many features of the mechanism are preserved despite the different catalytic components.
About this Structure
1USL is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Ribose-5-phosphate isomerase, with EC number 5.3.1.6 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site., Roos AK, Andersson CE, Bergfors T, Jacobsson M, Karlen A, Unge T, Jones TA, Mowbray SL, J Mol Biol. 2004 Jan 16;335(3):799-809. PMID:14687575
Page seeded by OCA on Thu Feb 21 15:28:00 2008
Categories: Mycobacterium tuberculosis | Ribose-5-phosphate isomerase | Single protein | Andersson, C E. | Jones, T A. | Mowbray, S L. | Roos, A K. | SPINE, Structural Proteomics in Europe. | Unge, T. | PO4 | Isomerase | Pentose phosphate pathway | Phosphopentose isomerase b | Phosphoriboisomerase b | Rv2465c | Spine | Structural genomics | Structural proteomics in europe
