255l
From Proteopedia
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| - | [[Image:255l.jpg|left|200px]] | + | [[Image:255l.jpg|left|200px]] |
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| - | '''HYDROLASE''' | + | {{Structure |
| + | |PDB= 255l |SIZE=350|CAPTION= <scene name='initialview01'>255l</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | ||
| + | |GENE= T4 LYSOZYME GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | ||
| + | }} | ||
| + | |||
| + | '''HYDROLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 255L is a [ | + | 255L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=255L OCA]. |
==Reference== | ==Reference== | ||
| - | A relationship between protein stability and protein function., Shoichet BK, Baase WA, Kuroki R, Matthews BW, Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):452-6. PMID:[http:// | + | A relationship between protein stability and protein function., Shoichet BK, Baase WA, Kuroki R, Matthews BW, Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):452-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7831309 7831309] |
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:43:11 2008'' |
Revision as of 13:43, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | T4 LYSOZYME GENE (Bacteriophage T4) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDROLASE
Overview
Enzymes are thought to use their ordered structures to facilitate catalysis. A corollary of this theory suggests that enzyme residues involved in function are not optimized for stability. We tested this hypothesis by mutating functionally important residues in the active site of T4 lysozyme. Six mutations at two catalytic residues, Glu-11 and Asp-20, abolished or reduced enzymatic activity but increased thermal stability by 0.7-1.7 kcal.mol-1. Nine mutations at two substrate-binding residues, Ser-117 and Asn-132, increased stability by 1.2-2.0 kcal.mol-1, again at the cost of reduced activity. X-ray crystal structures show that the substituted residues complement regions of the protein surface that are used for substrate recognition in the native enzyme. In two of these structures the enzyme undergoes a general conformational change, similar to that seen in an enzyme-product complex. These results support a relationship between stability and function for T4 lysozyme. Other evidence suggests that the relationship is general.
About this Structure
255L is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
A relationship between protein stability and protein function., Shoichet BK, Baase WA, Kuroki R, Matthews BW, Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):452-6. PMID:7831309
Page seeded by OCA on Thu Mar 20 15:43:11 2008
