2ch2
From Proteopedia
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| - | [[Image:2ch2.gif|left|200px]]<br /><applet load="2ch2" size=" | + | [[Image:2ch2.gif|left|200px]]<br /><applet load="2ch2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ch2, resolution 2.70Å" /> | caption="2ch2, resolution 2.70Å" /> | ||
'''STRUCTURE OF THE ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE IN COMPLEX WITH INHIBITOR'''<br /> | '''STRUCTURE OF THE ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE IN COMPLEX WITH INHIBITOR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CH2 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 KY1, LLP and KY1 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ky1 Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2CH2 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 <scene name='pdbligand=KY1:'>KY1</scene>, <scene name='pdbligand=LLP:'>LLP</scene> and <scene name='pdbligand=KY1:'>KY1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ky1+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:35:13 2008'' |
Revision as of 08:35, 3 February 2008
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STRUCTURE OF THE ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE IN COMPLEX WITH INHIBITOR
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
2CH2 is a Single protein structure of sequence from Anopheles gambiae with , and 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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