1gkm

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[[Image:1gkm.gif|left|200px]]
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{{STRUCTURE_1gkm| PDB=1gkm | SCENE= }}
{{STRUCTURE_1gkm| PDB=1gkm | SCENE= }}
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'''HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE'''
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===HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE===
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==Overview==
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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--&gt;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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11895450}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11895450 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11895450}}
==About this Structure==
==About this Structure==
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[[Category: Histidine degradation]]
[[Category: Histidine degradation]]
[[Category: Lyase]]
[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:41:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:26:42 2008''

Revision as of 02:26, 1 July 2008

Image:1gkm.png

Template:STRUCTURE 1gkm

HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE

Template:ABSTRACT PUBMED 11895450

About this Structure

1GKM 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

Page seeded by OCA on Tue Jul 1 05:26:42 2008

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