Aspartate-semialdehyde dehydrogenase

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[[Image:1mc4.png|left|200px|thumb|Crystal Structure of Aspartate-semialdehyde dehydrogenase, [[1mc4]]]]
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<StructureSection load='1mb4' size='350' side='right' caption='Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code [[1mb4]])' scene='45/452498/Cv/2'>
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{{STRUCTURE_1mc4| PDB=1mc4 | SIZE=400| SCENE=Aspartate-semialdehyde_dehydrogenase/Cv/1 |right|CAPTION=Aspartate-semialdehyde dehydrogenase, [[1mc4]] }}
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[[Aspartate-semialdehyde dehydrogenase]] (ASADH) is an enzyme which is part of the biosynthesis of amino acids. It catalyzes the conversion of L-aspartate 4-semialdehyde (ASA) + phosphate + NADP to L-4-aspartyl phosphate + NADPH + H+. The images at the left and at the right correspond to one representative ASADH, ''i.e.'' the crystal structure of Aspartate-semialdehyde dehydrogenase from ''Vibrio cholerae'' ([[1mc4]]).
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== Function ==
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{{TOC limit|limit=2}}
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'''Aspartate-semialdehyde dehydrogenase''' (ASADH) is an enzyme which is part of the biosynthesis of amino acids in bacteria, plants and fungi. It catalyzes the conversion of L-aspartate 4-semialdehyde (ASA) + phosphate + NADP to L-4-aspartyl phosphate + NADPH + H+.
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== 3D Structures of Aspartate-semialdehyde dehydrogenase ==
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== Structural highlights ==
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[[2qz9]], [[1mc4]] – VcASADH II – ''Vibrio cholerae''<br />
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ASADH contains 2 domains. The N terminal domain contains the <scene name='45/452498/Cv/7'>active site</scene> and the <scene name='45/452498/Cv/9'>NADP-binding site</scene>. The active site contains a <scene name='45/452498/Cv/10'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
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[[2yv3]] – ASADH – ''Thermus thermiphilus''<br />
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[[1t4d]], [[1t4b]], [[1brm]] - EcASADH β - ''Escherichia coli''<br />
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[[1pu2]], [[1oza]] - HiASADH (mutant) – ''Haemophilus influenzae''<br />
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[[1nwc]] – HiASADH<br />
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[[1nwh]] – HiASADH reaction intermediate<br />
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===ASADH binary complex===
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== 3D Structures of Aspartate-semialdehyde dehydrogenase ==
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[[Aspartate-semialdehyde dehydrogenase 3D structures]]
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[[2r00]] - VcASADH II + ASA<br />
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[[3llg]] – ASADH + glycerot + Pi – ''Mycobacterium tuberculosis''<br />
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[[3hsk]] – ASADH + NADP – ''Candida albicans''<br />
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[[1ys4]] - ASADH + NADP – ''Methanocaldococcus jannaschii''<br />
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[[1nx6]] - HiASADH reaction intermediate +Pi<br />
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[[1ta4]] - HiASADH + As<br />
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[[1tb4]] - HiASADH + IO4<br />
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[[1q2x]] - HiASADH (mutant) + ASA<br />
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===ASADH ternary complex===
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[[1pqu]] - HiASADH (mutant) + NADP + cacodylate + substrate analog<br />
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</StructureSection>
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[[1pqp]] - HiASADH (mutant) + ASA + Pi<br />
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[[1gl3]] - EcASADH β + NADP + substrate analog<br />
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[[1mb4]] - VcASADH + NADP + substrate analog<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code 1mb4)

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References

  1. Blanco J, Moore RA, Kabaleeswaran V, Viola RE. A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. Protein Sci. 2003 Jan;12(1):27-33. PMID:12493825

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Michal Harel, Alexander Berchansky

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