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2ch1
From Proteopedia
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| - | [[Image:2ch1.gif|left|200px]]<br /> | + | [[Image:2ch1.gif|left|200px]]<br /><applet load="2ch1" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ch1" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2ch1, resolution 2.40Å" /> | caption="2ch1, resolution 2.40Å" /> | ||
'''STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE'''<br /> | '''STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae] with LLP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2CH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae] with LLP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CH1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:22:37 2007'' |
Revision as of 17:12, 18 December 2007
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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 with LLP and GOL as ligands. Known structural/functional Site: . 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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