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1gkm

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[[Image:1gkm.gif|left|200px]]<br /><applet load="1gkm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gkm.gif|left|200px]]
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caption="1gkm, resolution 1.0&Aring;" />
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'''HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE'''<br />
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{{Structure
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|PDB= 1gkm |SIZE=350|CAPTION= <scene name='initialview01'>1gkm</scene>, resolution 1.0&Aring;
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|SITE= <scene name='pdbsite=MIO:Modification+Forming+The+Catalytically+Essential+Electro+...'>MIO</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GKM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CYS:'>CYS</scene>, <scene name='pdbligand=O:'>O</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=MIO:Modification+Forming+The+Catalytically+Essential+Electro+...'>MIO</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKM OCA].
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1GKM 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=1GKM OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11895450 11895450]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:23 2008''

Revision as of 09:24, 20 March 2008

Image:1gkm.gif


PDB ID 1gkm

Drag the structure with the mouse to rotate
, resolution 1.0Å
Sites:
Ligands: , , and
Activity: Histidine ammonia-lyase, with EC number 4.3.1.3
Coordinates: save as pdb, mmCIF, xml



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


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

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 Thu Mar 20 11:24:23 2008

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