1gkj
From Proteopedia
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| - | [[Image:1gkj.gif|left|200px]] | + | [[Image:1gkj.gif|left|200px]] |
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| - | '''HISTIDINE AMMONIA-LYASE (HAL) MUTANT Y280F FROM PSEUDOMONAS PUTIDA''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HISTIDINE AMMONIA-LYASE (HAL) MUTANT Y280F FROM PSEUDOMONAS PUTIDA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GKJ is a [ | + | 1GKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKJ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11895450 11895450] |
[[Category: Histidine ammonia-lyase]] | [[Category: Histidine ammonia-lyase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:20 2008'' |
Revision as of 09:24, 20 March 2008
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| , resolution 1.7Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Histidine ammonia-lyase, with EC number 4.3.1.3 | ||||||
| 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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