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| - | [[Image:1laa.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1laa| PDB=1laa | SCENE= }} | | {{STRUCTURE_1laa| PDB=1laa | SCENE= }} |
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| - | '''X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME'''
| + | ===X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME=== |
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| - | ==Overview==
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| - | The three-dimensional structure of a modified human lysozyme (HL), Glu 53 HL, in which Asp 53 was replaced by Glu, has been determined at 1.77 A resolution by X-ray analysis. The backbone structure of Glu 53 HL is essentially the same as the structure of wild-type HL. The root mean square difference for the superposition of equivalent C alpha atoms is 0.141 A. Except for the Glu 53 residue, the structure of the active site region is largely conserved between Glu 53 HL and wild-type HL. However, the hydrogen bond network differs because of the small shift or rotation of side chain groups. The carboxyl group of Glu 53 points to the carboxyl group of Glu 35 with a distance of 4.7 A between the nearest carboxyl oxygen atoms. A water molecule links these carboxyl groups by a hydrogen bond bridge. The active site structure explains well the fact that the binding ability for substrates does not significantly differ between Glu 53 HL and wild-type HL. On the other hand, the positional and orientational change of the carboxyl group of the residue 53 caused by the mutation is considered to be responsible for the low catalytic activity (ca. 1%) of Glu 53 HL. The requirement of precise positioning for the carboxyl group suggests the possibility that the Glu 53 residue contributes more than a simple electrostatic stabilization of the intermediate in the catalysis reaction.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_1363898}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1363898 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1363898}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Jigami, Y.]] | | [[Category: Jigami, Y.]] |
| | [[Category: Muraki, M.]] | | [[Category: Muraki, M.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:43:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:06:22 2008'' |
Revision as of 09:06, 2 July 2008
Template:STRUCTURE 1laa
X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME
Template:ABSTRACT PUBMED 1363898
About this Structure
1LAA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structure of Glu 53 human lysozyme., Harata K, Muraki M, Hayashi Y, Jigami Y, Protein Sci. 1992 Nov;1(11):1447-53. PMID:1363898
Page seeded by OCA on Wed Jul 2 12:06:22 2008
