1usl

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[[Image:1usl.jpg|left|200px]]<br /><applet load="1usl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1usl.jpg|left|200px]]
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caption="1usl, resolution 1.88&Aring;" />
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'''STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE.'''<br />
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{{Structure
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|PDB= 1usl |SIZE=350|CAPTION= <scene name='initialview01'>1usl</scene>, resolution 1.88&Aring;
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|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+E'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6]
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|GENE=
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}}
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'''STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, COMPLEXED WITH PHOSPHATE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1USL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] Known structural/functional Site: <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+E'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USL OCA].
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1USL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USL OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14687575 14687575]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14687575 14687575]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Ribose-5-phosphate isomerase]]
[[Category: Ribose-5-phosphate isomerase]]
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[[Category: rv2465c]]
[[Category: rv2465c]]
[[Category: spine]]
[[Category: spine]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:36:15 2008''

Revision as of 12:36, 20 March 2008

Image:1usl.jpg


PDB ID 1usl

Drag the structure with the mouse to rotate
, resolution 1.88Å
Sites:
Ligands:
Activity: Ribose-5-phosphate isomerase, with EC number 5.3.1.6
Coordinates: save as pdb, mmCIF, xml



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. 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

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