1gkj
From Proteopedia
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|PDB= 1gkj |SIZE=350|CAPTION= <scene name='initialview01'>1gkj</scene>, resolution 1.7Å | |PDB= 1gkj |SIZE=350|CAPTION= <scene name='initialview01'>1gkj</scene>, resolution 1.7Å | ||
|SITE= <scene name='pdbsite=MIO:Modification+Forming+The+Catalytically+Essential+Electro+...'>MIO</scene> | |SITE= <scene name='pdbsite=MIO:Modification+Forming+The+Catalytically+Essential+Electro+...'>MIO</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gkj OCA], [http://www.ebi.ac.uk/pdbsum/1gkj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gkj RCSB]</span> | ||
}} | }} | ||
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[[Category: Baedeker, M.]] | [[Category: Baedeker, M.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: ammonia-lyase]] | [[Category: ammonia-lyase]] | ||
[[Category: histidine degradation]] | [[Category: histidine degradation]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''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 20:46:02 2008'' |
Revision as of 17:46, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Histidine ammonia-lyase, with EC number 4.3.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HISTIDINE AMMONIA-LYASE (HAL) MUTANT Y280F FROM PSEUDOMONAS PUTIDA
Overview
Histidine ammonia-lyase (EC 4.3.1.3) catalyzes the nonoxidative elimination of the alpha-amino group of histidine using a 4-methylidene-imidazole-5-one (MIO), which is formed autocatalytically from the internal peptide segment 142Ala-Ser-Gly. The structure of the enzyme inhibited by a reaction with l-cysteine was established at the very high resolution of 1.0 A. Five active center mutants were produced and their catalytic activities were measured. Among them, mutant Tyr280-->Phe could be crystallized and its structure could be determined at 1.7 A resolution. It contains a planar sp2-hybridized 144-N atom of MIO, in contrast to the pyramidal sp3-hybridized 144-N of the wild-type. With the planar 144-N atom, MIO assumes the conformation of a putative intermediate aromatic state of the reaction, demonstrating that the conformational barrier between aromatic and wild-type states is very low. The data led to a new proposal for the geometry for the catalyzed reaction, which also applies to the closely related phenylalanine ammonia-lyase (EC 4.3.1.5). Moreover, it suggested an intermediate binding site for the released ammonia.
About this Structure
1GKJ is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism., Baedeker M, Schulz GE, Eur J Biochem. 2002 Mar;269(6):1790-7. PMID:11895450
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