153l: Difference between revisions

Revision as of 12:38, 21 February 2008

THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE

OverviewOverview

The structure of goose egg-white lysozyme (GEWL) has been refined to an R-value of 15.9% at 1.6 A resolution. Details of the structure determination, the refinement and the structure itself are presented. The structure of a complex of the enzyme with the trisaccharide of N-acetyl glucosamine has also been determined and refined at 1.6 A resolution. The trisaccharide occupies sites analogous to the B, C and D subsites of chicken (HEWL) and phage T4 (T4L) lysozymes. All three lysozymes (GEWL, HEWL and T4L) display the same characteristic set of bridging hydrogen bonds between backbone atoms of the protein and the 2-acetamido group of the saccharide in subsite C. Glu73 of GEWL is seen to correspond closely to Glu35 of HEWL (and to Glu11 of T4L) and supports the established view that this group is critically involved in the catalytic mechanism. There is, however, no obvious residue in goose lysozyme that is a counterpart of Asp52 of chicken lysozyme (or of Asp20 in T4L), suggesting that a second acidic residue is not essential for the catalytic activity of goose lysozyme, and may not be required for the activity of other lysozymes.

About this StructureAbout this Structure

153L is a Single protein structure of sequence from [1]. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue., Weaver LH, Grutter MG, Matthews BW, J Mol Biol. 1995 Jan 6;245(1):54-68. PMID:7823320

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-[[Image:153l.jpg|left|200px]]<br /><applet load="153l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:153l.jpg|left|200px]]<br /><applet load="153l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="153l, resolution 1.6&Aring;" />
 '''THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE'''<br />
 ==Overview==
-The structure of goose egg-white lysozyme (GEWL) has been refined to an, R-value of 15.9% at 1.6 A resolution. Details of the structure, determination, the refinement and the structure itself are presented. The, structure of a complex of the enzyme with the trisaccharide of N-acetyl, glucosamine has also been determined and refined at 1.6 A resolution. The, trisaccharide occupies sites analogous to the B, C and D subsites of, chicken (HEWL) and phage T4 (T4L) lysozymes. All three lysozymes (GEWL, HEWL and T4L) display the same characteristic set of bridging hydrogen, bonds between backbone atoms of the protein and the 2-acetamido group of, the saccharide in subsite C. Glu73 of GEWL is seen to correspond closely, to Glu35 of HEWL (and to Glu11 of T4L) and supports the established view, that this group is critically involved in the catalytic mechanism. There, is, however, no obvious residue in goose lysozyme that is a counterpart of, Asp52 of chicken lysozyme (or of Asp20 in T4L), suggesting that a second, acidic residue is not essential for the catalytic activity of goose, lysozyme, and may not be required for the activity of other lysozymes.
+The structure of goose egg-white lysozyme (GEWL) has been refined to an R-value of 15.9% at 1.6 A resolution. Details of the structure determination, the refinement and the structure itself are presented. The structure of a complex of the enzyme with the trisaccharide of N-acetyl glucosamine has also been determined and refined at 1.6 A resolution. The trisaccharide occupies sites analogous to the B, C and D subsites of chicken (HEWL) and phage T4 (T4L) lysozymes. All three lysozymes (GEWL, HEWL and T4L) display the same characteristic set of bridging hydrogen bonds between backbone atoms of the protein and the 2-acetamido group of the saccharide in subsite C. Glu73 of GEWL is seen to correspond closely to Glu35 of HEWL (and to Glu11 of T4L) and supports the established view that this group is critically involved in the catalytic mechanism. There is, however, no obvious residue in goose lysozyme that is a counterpart of Asp52 of chicken lysozyme (or of Asp20 in T4L), suggesting that a second acidic residue is not essential for the catalytic activity of goose lysozyme, and may not be required for the activity of other lysozymes.
 ==About this Structure==
-L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=153L OCA].
+L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=153L OCA].
 ==Reference==
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 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Gruetter, M.G.]]
+[[Category: Gruetter, M G.]]
-[[Category: Matthews, B.W.]]
+[[Category: Matthews, B W.]]
-[[Category: Weaver, L.H.]]
+[[Category: Weaver, L H.]]
 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:27:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:38:28 2008''