1o5x
From Proteopedia
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|PDB= 1o5x |SIZE=350|CAPTION= <scene name='initialview01'>1o5x</scene>, resolution 1.10Å | |PDB= 1o5x |SIZE=350|CAPTION= <scene name='initialview01'>1o5x</scene>, resolution 1.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o5x OCA], [http://www.ebi.ac.uk/pdbsum/1o5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o5x RCSB]</span> | ||
}} | }} | ||
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[[Category: Murthy, M R.]] | [[Category: Murthy, M R.]] | ||
[[Category: Parthasarathy, S.]] | [[Category: Parthasarathy, S.]] | ||
| - | [[Category: 2PG]] | ||
| - | [[Category: 3PY]] | ||
| - | [[Category: PO3]] | ||
[[Category: 2-phosphoglycerate]] | [[Category: 2-phosphoglycerate]] | ||
[[Category: catalytic loop6]] | [[Category: catalytic loop6]] | ||
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[[Category: triosephosphate isomerase]] | [[Category: triosephosphate isomerase]] | ||
| - | ''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 22:40:20 2008'' |
Revision as of 19:40, 30 March 2008
| |||||||
| , resolution 1.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Plasmodium falciparum TIM complexed to 2-phosphoglycerate
Overview
Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and glyceraldehyde 3-phosphate. In this communication we report the crystal structure of Plasmodium falciparum triose-phosphate isomerase complexed to the inhibitor 2-phosphoglycerate at 1.1-A resolution. The crystallographic asymmetric unit contains a dimeric molecule. The inhibitor bound to one of the subunits in which the flexible catalytic loop 6 is in the open conformation has been cleaved into two fragments presumably due to radiation damage. The cleavage products have been tentatively identified as 2-oxoglycerate and meta-phosphate. The intact 2-phosphoglycerate bound to the active site of the other subunit has been observed in two different orientations. The active site loop in this subunit is in both open and "closed" conformations, although the open form is predominant. Concomitant with the loop closure, Phe-96, Leu-167, and residues 208-211 (YGGS) are also observed in dual conformations in the B-subunit. Detailed comparison of the active-site geometry in the present case to the Saccharomyces cerevisiae triose-phosphate isomerase-dihydroxy acetone phosphate and Leishmania mexicana triose-phosphate isomerase-phosphoglycolate complexes, which have also been determined at atomic resolution, shows that certain interactions are common to the three structures, although 2-phosphoglycerate is neither a substrate nor a transition state analogue.
About this Structure
1O5X is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution., Parthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR, J Biol Chem. 2003 Dec 26;278(52):52461-70. Epub 2003 Oct 16. PMID:14563846
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