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1h19
From Proteopedia
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|PDB= 1h19 |SIZE=350|CAPTION= <scene name='initialview01'>1h19</scene>, resolution 2.1Å | |PDB= 1h19 |SIZE=350|CAPTION= <scene name='initialview01'>1h19</scene>, resolution 2.1Å | ||
|SITE= <scene name='pdbsite=ZN1:Imd+Binding+Site+For+Chain+A'>ZN1</scene> | |SITE= <scene name='pdbsite=ZN1:Imd+Binding+Site+For+Chain+A'>ZN1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h19 OCA], [http://www.ebi.ac.uk/pdbsum/1h19 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h19 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tholander, F.]] | [[Category: Tholander, F.]] | ||
[[Category: Thunnissen, M M.G M.]] | [[Category: Thunnissen, M M.G M.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: IMD]] | ||
| - | [[Category: YB]] | ||
| - | [[Category: ZN]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:44 2008'' |
Revision as of 17:55, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Leukotriene-A(4) hydrolase, with EC number 3.3.2.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF [E271Q] LEUKOTRIENE A4 HYDROLASE
Overview
Leukotriene A(4) hydrolase/aminopeptidase is a bifunctional zinc metalloenzyme that converts the fatty acid epoxide leukotriene A(4) into leukotriene B(4), a potent chemoattractant and immune-modulating lipid mediator. Recently, the structure of leukotriene A(4) hydrolase revealed that Glu-271, which belongs to a conserved GXMEN motif in the M1 family of zinc peptidases, and Gln-136 are located at the active site. Here we report that mutagenetic replacements of Glu-271, but not Gln-136, abrogate both catalytic activities of leukotriene A(4) hydrolase. Furthermore, the 2.1 A crystal structure of [E271Q]leukotriene A(4) hydrolase revealed minimal conformational changes that could not explain the loss of enzyme function. We propose that the carboxylate of Glu-271 participates in an acid-induced opening of the epoxide moiety of leukotriene A(4) and formation of a carbocation intermediate. Moreover, Glu-271 appears to act as an N-terminal recognition site and may potentially stabilize the transition-state during turnover of peptides, a property that most likely pertains to all members of the M1 family of zinc aminopeptidases. Hence, Glu-271 is a unique example of an amino acid, which has dual and separate functions in two different catalytic reactions, involving lipid and peptide substrates, respectively.
About this Structure
1H19 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:11675384
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