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2ch1

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[[Image:2ch1.gif|left|200px]]
[[Image:2ch1.gif|left|200px]]
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{{Structure
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|PDB= 2ch1 |SIZE=350|CAPTION= <scene name='initialview01'>2ch1</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2ch1", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+D'>AC1</scene>
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|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>
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{{STRUCTURE_2ch1| PDB=2ch1 | SCENE= }}
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|RELATEDENTRY=
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|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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'''STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE'''
'''STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE'''
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[[Category: Rossi, F.]]
[[Category: Rossi, F.]]
[[Category: 3-hydroxykynurenine transaminase]]
[[Category: 3-hydroxykynurenine transaminase]]
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[[Category: anopheles gambiae]]
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[[Category: Anopheles gambiae]]
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[[Category: kynurenine pathway]]
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[[Category: Kynurenine pathway]]
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[[Category: plp-enzyme]]
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[[Category: Plp-enzyme]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:07:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:19 2008''
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Revision as of 19:07, 3 May 2008

Template:STRUCTURE 2ch1

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 Page seeded by OCA on Sat May 3 22:07:18 2008

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