1u2p

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|PDB= 1u2p |SIZE=350|CAPTION= <scene name='initialview01'>1u2p</scene>, resolution 1.90&Aring;
|PDB= 1u2p |SIZE=350|CAPTION= <scene name='initialview01'>1u2p</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span>
|GENE= MPTPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|GENE= MPTPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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|DOMAIN=
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|RELATEDENTRY=[[1u2q|1U2Q]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2p OCA], [http://www.ebi.ac.uk/pdbsum/1u2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u2p RCSB]</span>
}}
}}
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[[Category: Sankaranarayanan, R.]]
[[Category: Sankaranarayanan, R.]]
[[Category: Wiker, H G.]]
[[Category: Wiker, H G.]]
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[[Category: CL]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: mycobacterium]]
[[Category: mycobacterium]]
[[Category: tyrosine phosphatase]]
[[Category: tyrosine phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:26:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:34 2008''

Revision as of 21:04, 30 March 2008


PDB ID 1u2p

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Gene: MPTPA (Mycobacterium tuberculosis)
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Related: 1U2Q


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Mycobacterium tuberculosis Low Molecular Protein Tyrosine Phosphatase (MPtpA) at 1.9A resolution


Overview

The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs to a distinctive class of phosphotyrosine phosphatases widely distributed among prokaryotes and eukaryotes. We report here the crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis. The structure was determined to be two crystal forms at 1.9- and 2.5-A resolutions. These structural forms are compared with those of the LMWPTPases of eukaryotes. Though the overall structure resembles that of the eukaryotic LMWPTPases, there are significant changes around the active site and the protein tyrosine phosphatase (PTP) loop. The variable loop forming the wall of the crevice leading to the active site is conformationally unchanged from that of mammalian LMWPTPase; however, differences are observed in the residues involved, suggesting that they have a role in influencing different substrate specificities. The single amino acid substitution (Leu12Thr [underlined below]) in the consensus sequence of the PTP loop, CTGNICRS, has a major role in the stabilization of the PTP loop, unlike what occurs in mammalian LMWPTPases. A chloride ion and a glycerol molecule were modeled in the active site where the chloride ion interacts in a manner similar to that of phosphate with the main chain nitrogens of the PTP loop. This structural study, in addition to identifying specific mycobacterial features, may also form the basis for exploring the mechanism of the substrate specificities of bacterial LMWPTPases.

About this Structure

1U2P is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution., Madhurantakam C, Rajakumara E, Mazumdar PA, Saha B, Mitra D, Wiker HG, Sankaranarayanan R, Das AK, J Bacteriol. 2005 Mar;187(6):2175-81. PMID:15743966

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