2huu: Difference between revisions

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[[Image:2huu.gif|left|200px]]<br /><applet load="2huu" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2huu.gif|left|200px]]
caption="2huu, resolution 2.100&Aring;" />
 
'''Crystal structure of Aedes aegypti alanine glyoxylate aminotransferase in complex with alanine'''<br />
{{Structure
|PDB= 2huu |SIZE=350|CAPTION= <scene name='initialview01'>2huu</scene>, resolution 2.100&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ALA:ALANINE'>ALA</scene> and <scene name='pdbligand=1BO:1-BUTANOL'>1BO</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44]
|GENE=
}}
 
'''Crystal structure of Aedes aegypti alanine glyoxylate aminotransferase in complex with alanine'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
2HUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti] with <scene name='pdbligand=ALA:'>ALA</scene> and <scene name='pdbligand=1BO:'>1BO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUU OCA].  
2HUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUU OCA].  


==Reference==
==Reference==
Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase., Han Q, Robinson H, Gao YG, Vogelaar N, Wilson SR, Rizzi M, Li J, J Biol Chem. 2006 Dec 1;281(48):37175-82. Epub 2006 Sep 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16990263 16990263]
Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase., Han Q, Robinson H, Gao YG, Vogelaar N, Wilson SR, Rizzi M, Li J, J Biol Chem. 2006 Dec 1;281(48):37175-82. Epub 2006 Sep 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16990263 16990263]
[[Category: Aedes aegypti]]
[[Category: Aedes aegypti]]
[[Category: Alanine--glyoxylate transaminase]]
[[Category: Alanine--glyoxylate transaminase]]
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[[Category: plp-dependent transferase]]
[[Category: plp-dependent transferase]]


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Revision as of 18:21, 20 March 2008

File:2huu.gif


PDB ID 2huu

Drag the structure with the mouse to rotate
, resolution 2.100Å
Ligands: and
Activity: Alanine--glyoxylate transaminase, with EC number 2.6.1.44
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Aedes aegypti alanine glyoxylate aminotransferase in complex with alanine


OverviewOverview

Mosquitoes are unique in having evolved two alanine glyoxylate aminotransferases (AGTs). One is 3-hydroxykynurenine transaminase (HKT), which is primarily responsible for catalyzing the transamination of 3-hydroxykynurenine (3-HK) to xanthurenic acid (XA). Interestingly, XA is used by malaria parasites as a chemical trigger for their development within the mosquito. This 3-HK to XA conversion is considered the major mechanism mosquitoes use to detoxify the chemically reactive and potentially toxic 3-HK. The other AGT is a typical dipteran insect AGT and is specific for converting glyoxylic acid to glycine. Here we report the 1.75A high-resolution three-dimensional crystal structure of AGT from the mosquito Aedes aegypti (AeAGT) and structures of its complexes with reactants glyoxylic acid and alanine at 1.75 and 2.1A resolution, respectively. This is the first time that the three-dimensional crystal structures of an AGT with its amino acceptor, glyoxylic acid, and amino donor, alanine, have been determined. The protein is dimeric and adopts the type I-fold of pyridoxal 5-phosphate (PLP)-dependent aminotransferases. The PLP co-factor is covalently bound to the active site in the crystal structure, and its binding site is similar to those of other AGTs. The comparison of the AeAGT-glyoxylic acid structure with other AGT structures revealed that these glyoxylic acid binding residues are conserved in most AGTs. Comparison of the AeAGT-alanine structure with that of the Anopheles HKT-inhibitor complex suggests that a Ser-Asn-Phe motif in the latter may be responsible for the substrate specificity of HKT enzymes for 3-HK.

About this StructureAbout this Structure

2HUU is a Single protein structure of sequence from Aedes aegypti. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase., Han Q, Robinson H, Gao YG, Vogelaar N, Wilson SR, Rizzi M, Li J, J Biol Chem. 2006 Dec 1;281(48):37175-82. Epub 2006 Sep 21. PMID:16990263

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