253l: Difference between revisions
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|PDB= 253l |SIZE=350|CAPTION= <scene name='initialview01'>253l</scene>, resolution 2.0Å | |PDB= 253l |SIZE=350|CAPTION= <scene name='initialview01'>253l</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= T4 LYSOZYME GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | |GENE= T4 LYSOZYME GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=253l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=253l OCA], [http://www.ebi.ac.uk/pdbsum/253l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=253l RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
253L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 253L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=253L 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://www.ncbi.nlm.nih.gov/pubmed/7831309 7831309] | 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: | [[Category: Enterobacteria phage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Shoichet, B.]] | [[Category: Shoichet, B.]] | ||
[[Category: Weaver, L H.]] | [[Category: Weaver, L H.]] | ||
[[Category: bacteriolytic enzyme]] | [[Category: bacteriolytic enzyme]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:45:25 2008'' | ||
Revision as of 01:45, 31 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | T4 LYSOZYME GENE (Enterobacteria phage T4) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LYSOZYME
OverviewOverview
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 StructureAbout this Structure
253L is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
ReferenceReference
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
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