1n2l: Difference between revisions

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[[Image:1n2l.jpg|left|200px]]
[[Image:1n2l.jpg|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1n2l", creates the "Structure Box" on the page.
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FGP:2-AMINO-3-HYDROXY-3-PHOSPHONOOXY-PROPIONIC+ACID'>FGP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cerebroside-sulfatase Cerebroside-sulfatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.6.8 3.1.6.8] </span>
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{{STRUCTURE_1n2l| PDB=1n2l  | SCENE= }}  
|RELATEDENTRY=[[1n2k|1N2K]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n2l OCA], [http://www.ebi.ac.uk/pdbsum/1n2l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n2l RCSB]</span>
}}


'''Crystal structure of a covalent intermediate of endogenous human arylsulfatase A'''
'''Crystal structure of a covalent intermediate of endogenous human arylsulfatase A'''
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[[Category: Monkiewicz, M.]]
[[Category: Monkiewicz, M.]]
[[Category: Ortlund, E.]]
[[Category: Ortlund, E.]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: inhibition]]
[[Category: Inhibition]]
[[Category: lysosomal enzyme]]
[[Category: Lysosomal enzyme]]
[[Category: metal ion]]
[[Category: Metal ion]]
[[Category: modified formylglycine]]
[[Category: Modified formylglycine]]
[[Category: phosphate ester hydrolysis]]
[[Category: Phosphate ester hydrolysis]]
 
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Revision as of 02:00, 3 May 2008

File:1n2l.jpg

Template:STRUCTURE 1n2l

Crystal structure of a covalent intermediate of endogenous human arylsulfatase A


OverviewOverview

The structures of human arylsulfatase A crystals soaked in solutions containing 4-methylumbelliferyl phosphate and O-phospho-DL-tyrosine have been determined at 2.7- and 3.2-A resolution, respectively. The formylglycine in position 69, a residue crucial for catalytic activity, was unambiguously identified in both structures as forming a covalent bond to the phosphate moiety. A hydroxyl group is present at the Cbeta of residue 69 and the formation of one out of two possible stereomeric forms is strongly favoured. The structures confirm the importance of the gem-diol intermediate in the arylsulfatase's catalytic mechanism. The presence of an apparently stable covalent bond is consistent with the weak phosphatase activity observed for human arylsulfatase A. The structures of the complexes suggest that phosphate ions and phosphate esters inhibit arylsulfatase in non-covalent and covalent modes, respectively. The metal ion present in the active site of arylsulfatase A isolated from human placenta is Ca(2+) and not Mg(2+) as was found in the structure of the recombinant enzyme.

About this StructureAbout this Structure

1N2L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a covalent intermediate of endogenous human arylsulfatase A., Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, Lewinski K, J Inorg Biochem. 2003 Aug 1;96(2-3):386-92. PMID:12888274 Page seeded by OCA on Sat May 3 02:00:47 2008

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