1jef: Difference between revisions

Revision as of 14:21, 21 February 2008

TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3

OverviewOverview

The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.

About this StructureAbout this Structure

1JEF is a Single protein structure of sequence from Meleagris gallopavo with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A., Harata K, Muraki M, Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):650-7. PMID:15299852

Page seeded by OCA on Thu Feb 21 13:21:44 2008

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-[[Image:1jef.gif|left|200px]]<br /><applet load="1jef" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jef.gif|left|200px]]<br /><applet load="1jef" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jef, resolution 1.77&Aring;" />
 '''TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3'''<br />
 ==Overview==
-The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose, [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH, 4.2. The crystal structure was determined by molecular replacement and, refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3, molecule occupies the subsites A, B and C. At the subsites B and C, the, sugar residues are bound in a similar manner to that found in the hen-egg, lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A, is exposed to bulk solvent and has no contact with the protein molecule, because the active residue Asp101 in HEL is replaced by Gly in TEL. A, sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds, with the sugar residue and the guanidino group of Arg61, assisting the, binding of the sugar residue to subsite B. The active-site cleft of TEL is, narrower than that of native TEL, thus attaining the best fit of the, (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed, in relation to the catalytic properties of TEL. The result suggests that, the cleavage pattern of oligosaccharide substrates in the catalytic, reaction is regulated by the protein-sugar interaction at subsite A.
+The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.
 ==About this Structure==
-JEF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JEF OCA].
+JEF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JEF OCA].
 ==Reference==
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 [[Category: inhibitor complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:44 2008''