1m4n

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|PDB= 1m4n |SIZE=350|CAPTION= <scene name='initialview01'>1m4n</scene>, resolution 2.01&Aring;
|PDB= 1m4n |SIZE=350|CAPTION= <scene name='initialview01'>1m4n</scene>, resolution 2.01&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=AAD:(2-AMINOOXY-ETHYL)-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL]-METHYL-SULFONIUM'>AAD</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene>
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|LIGAND= <scene name='pdbligand=AAD:(2-AMINOOXY-ETHYL)-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL]-METHYL-SULFONIUM'>AAD</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1b8g|1b8g]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4n OCA], [http://www.ebi.ac.uk/pdbsum/1m4n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m4n RCSB]</span>
}}
}}
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[[Category: Khomutov, R M.]]
[[Category: Khomutov, R M.]]
[[Category: Kirsch, J F.]]
[[Category: Kirsch, J F.]]
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[[Category: AAD]]
 
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[[Category: MES]]
 
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[[Category: PLP]]
 
[[Category: ethylene biosynthesis]]
[[Category: ethylene biosynthesis]]
[[Category: fruit ripening]]
[[Category: fruit ripening]]
[[Category: pyridoxal phosphate]]
[[Category: pyridoxal phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:42:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:12 2008''

Revision as of 19:11, 30 March 2008


PDB ID 1m4n

Drag the structure with the mouse to rotate
, resolution 2.01Å
Ligands: , ,
Activity: 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14
Related: 1b8g


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF APPLE ACC SYNTHASE IN COMPLEX WITH [2-(AMINO-OXY)ETHYL](5'-DEOXYADENOSIN-5'-YL)(METHYL)SULFONIUM


Overview

The crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with the substrate analogue [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium (AMA) was determined at 2.01-A resolution. The crystallographic results show that a covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of the natural substrate S-adenosyl-L-methionine (SAM)) and the pyridoxal 5'-phosphate (PLP) cofactor of ACC synthase. The oxime formation is supported by spectroscopic data. The ACC synthase-AMA structure provides reliable and detailed information on the binding mode of the natural substrate of ACC synthase and complements previous structural and functional work on this enzyme.

About this Structure

1M4N is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.

Reference

Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding., Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG, Biochim Biophys Acta. 2003 Apr 11;1647(1-2):55-60. PMID:12686108

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