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| - | [[Image:1wls.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1wls| PDB=1wls | SCENE= }} | | {{STRUCTURE_1wls| PDB=1wls | SCENE= }} |
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| - | '''Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii'''
| + | ===Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii=== |
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| - | ==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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15735339}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15735339 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15735339}} |
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| | ==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
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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