2ch1
From Proteopedia
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|PDB= 2ch1 |SIZE=350|CAPTION= <scene name='initialview01'>2ch1</scene>, resolution 2.40Å | |PDB= 2ch1 |SIZE=350|CAPTION= <scene name='initialview01'>2ch1</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ch1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch1 OCA], [http://www.ebi.ac.uk/pdbsum/2ch1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ch1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rizzi, M.]] | [[Category: Rizzi, M.]] | ||
[[Category: Rossi, F.]] | [[Category: Rossi, F.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: LLP]] | ||
[[Category: 3-hydroxykynurenine transaminase]] | [[Category: 3-hydroxykynurenine transaminase]] | ||
[[Category: anopheles gambiae]] | [[Category: anopheles gambiae]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:19 2008'' |
Revision as of 23:21, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE
Overview
In Anopheles gambiae, the vector for the most deadly malaria parasite Plasmodium falciparum, xanthurenic acid (XA) plays a key role in parasite gametogenesis and fertility. In mosquitoes, XA is produced by transamination of 3-hydroxykynurenine (3-HK), a reaction that represents the main route to prevent the accumulation of the potentially toxic 3-HK excess. Interfering with XA metabolism in A. gambiae therefore appears an attractive avenue for the development of malaria transmission-blocking drugs and insecticides. We have determined the crystal structure of A. gambiae 3-HK transaminase in its pyridoxal 5'-phosphate form and in complex with a newly synthesized competitive enzyme inhibitor. Structural inspection of the enzyme active site reveals the key molecular determinants for ligand recognition and catalysis. Major contributions toward inhibitor binding are provided by a salt bridge between the inhibitor carboxylate and Arg-356 and by a remarkable hydrogen bond network involving the anthranilic moiety of the inhibitor and backbone atoms of residues Gly-25 and Asn-44. This study may be useful for the structure-based design of specific enzyme inhibitors of potential interest as antimalarial agents.
About this Structure
2CH1 is a Single protein structure of sequence from Anopheles gambiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Anopheles gambiae 3-hydroxykynurenine transaminase., Rossi F, Garavaglia S, Giovenzana GB, Arca B, Li J, Rizzi M, Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5711-6. Epub 2006 Apr 3. PMID:16585514
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