1qtv

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|PDB= 1qtv |SIZE=350|CAPTION= <scene name='initialview01'>1qtv</scene>, resolution 2.3&Aring;
|PDB= 1qtv |SIZE=350|CAPTION= <scene name='initialview01'>1qtv</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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|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]
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|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=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1qtz|1QTZ]], [[1qt3|1QT3]], [[1qt4|1QT4]], [[1qt5|1QT5]], [[1qt6|1QT6]], [[1qt7|1QT7]], [[1qt8|1QT8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtv OCA], [http://www.ebi.ac.uk/pdbsum/1qtv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qtv RCSB]</span>
}}
}}
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==About this Structure==
==About this Structure==
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1QTV 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=1QTV OCA].
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1QTV 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=1QTV OCA].
==Reference==
==Reference==
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site., Kuroki R, Weaver LH, Matthews BW, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8949-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10430876 10430876]
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site., Kuroki R, Weaver LH, Matthews BW, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8949-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10430876 10430876]
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[[Category: Bacteriophage t4]]
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[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Weaver, L H.]]
[[Category: Weaver, L H.]]
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[[Category: BME]]
 
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[[Category: CL]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:56 2008''

Revision as of 20:18, 30 March 2008


PDB ID 1qtv

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: ,
Activity: Lysozyme, with EC number 3.2.1.17
Related: 1QTZ, 1QT3, 1QT4, 1QT5, 1QT6, 1QT7, 1QT8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



T26E APO STRUCTURE OF T4 LYSOZYME


Overview

In contrast to hen egg-white lysozyme, which retains the beta-configuration of the substrate in the product, T4 lysozyme (T4L) is an inverting glycosidase. The substitution Thr-26 --> His, however, converts T4L from an inverting to a retaining enzyme. It is shown here that the Thr-26 --> His mutant is also a transglycosidase. Indeed, the transglycosylation reaction can be more effective than hydrolysis. In contrast, wild-type T4L has no detectable transglycosidase activity. The results support the prior hypothesis that catalysis by the Thr-26 --> His mutant proceeds via a covalent intermediate. Further mutations (Glu-11 --> His, Asp-20 --> Cys) of the T26H mutant lysozyme indicate that the catalytic mechanism of this mutant requires Glu-11 as a general acid but Asp-20 is not essential. The results help provide an overall rationalization for the activity of glycosidases, in which a highly conserved acid group (Glu-11 in T4L, Glu-35 in hen egg-white lysozyme) on the beta-side of the substrate acts as a proton donor, whereas alterations in the placement and chemical identity of residues on the alpha-side of the substrate can lead to catalysis with or without retention of the configuration, to transglycosidase activity, or to the formation of a stable enzyme-substrate adduct.

About this Structure

1QTV is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site., Kuroki R, Weaver LH, Matthews BW, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8949-54. PMID:10430876

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