1gk3

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[[Image:1gk3.jpg|left|200px]]
[[Image:1gk3.jpg|left|200px]]
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{{Structure
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|PDB= 1gk3 |SIZE=350|CAPTION= <scene name='initialview01'>1gk3</scene>, resolution 2.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1gk3", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1gk3| PDB=1gk3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk3 OCA], [http://www.ebi.ac.uk/pdbsum/1gk3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gk3 RCSB]</span>
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'''HISTIDINE AMMONIA-LYASE (HAL) MUTANT D145A FROM PSEUDOMONAS PUTIDA'''
'''HISTIDINE AMMONIA-LYASE (HAL) MUTANT D145A FROM PSEUDOMONAS PUTIDA'''
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[[Category: Baedeker, M.]]
[[Category: Baedeker, M.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
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[[Category: ammonia-lyase]]
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[[Category: Ammonia-lyase]]
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[[Category: histidine degradation]]
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[[Category: Histidine degradation]]
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[[Category: lyase]]
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[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:40:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:45:47 2008''
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Revision as of 14:40, 2 May 2008

Image:1gk3.jpg

Template:STRUCTURE 1gk3

HISTIDINE AMMONIA-LYASE (HAL) MUTANT D145A FROM PSEUDOMONAS PUTIDA


Overview

Histidine ammonia-lyase requires a 4-methylidene-imidazole-5-one group (MIO) that is produced autocatalytically by a cyclization and dehydration step in a 3-residue loop of the polypeptide. The crystal structures of three mutants have been established. Two mutants were inactive and failed to form MIO, but remained unchanged elsewhere. The third mutant showed very low activity and formed MIO, although it differed from an MIO-less mutant only by an additional 329-C(beta) atom. This atom forms one constraint during MIO formation, the other being the strongly connected Asp145. An exploration of the conformational space of the MIO-forming loop showed that the cyclization is probably enforced by a mechanic compression in a late stage of chain folding and is catalyzed by a well-connected internal water molecule. The cyclization of the respective 3-residue loop of green fluorescent protein is likely to occur in a similar reaction.

About this Structure

1GK3 is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase., Baedeker M, Schulz GE, Structure. 2002 Jan;10(1):61-7. PMID:11796111 Page seeded by OCA on Fri May 2 17:40:35 2008

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