1wls: Difference between revisions

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[[Image:1wls.gif|left|200px]]
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[[Image:1wls.png|left|200px]]


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{{STRUCTURE_1wls|  PDB=1wls  |  SCENE=  }}  
{{STRUCTURE_1wls|  PDB=1wls  |  SCENE=  }}  


'''Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii'''
===Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii===




==Overview==
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The crystal structure of the L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii (PhA) was determined by the multiwavelength anomalous diffraction (MAD) method and was refined to a resolution of 2.16 angstroms with a crystallographic R factor and free R factor of 21.1 and 25.3%, respectively. This is the first report of the three-dimensional structure of a type I L-asparaginase. These enyzmes are known as cytosolic L-asparaginases with lower affinities for substrate than the type II L-asparaginases. Although the overall fold of PhA was closely related to the structure of the well characterized type II L-asparaginase, structural differences were also detected. PhA forms a homodimer that corresponds to half the homotetramer of type II L-asparaginases. Structure comparison at the active site reveals that most catalytic residues are conserved except for two residues that recognize the amino group of the substrate. Additionally, a remarkable structural difference is found in the so-called 'active-site flexible loop'. In PhA this loop is stabilized by beta-hairpin formation and by elaborate interactions with the type-I-specific alpha-helical region derived from the other subunit forming the PhA dimer. The flexible loop of the type II enzyme is considered to serve as a mobile gate to the active site. Therefore, the loop stabilization observed in the PhA structure may cause limitation of the access of the substrate to the active site.
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{{ABSTRACT_PUBMED_15735339}}


==About this Structure==
==About this Structure==
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[[Category: Yasutake, Y.]]
[[Category: Yasutake, Y.]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:51:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:19:25 2008''

Revision as of 09:19, 27 July 2008

File:1wls.png

Template:STRUCTURE 1wls

Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii

Template:ABSTRACT PUBMED 15735339

About this Structure

1WLS is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution., Yao M, Yasutake Y, Morita H, Tanaka I, Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):294-301. Epub 2005, Feb 24. PMID:15735339

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