1jef

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[[Image:1jef.gif|left|200px]]<br /><applet load="1jef" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jef.gif|left|200px]]
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caption="1jef, resolution 1.77&Aring;" />
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'''TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3'''<br />
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{{Structure
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|PDB= 1jef |SIZE=350|CAPTION= <scene name='initialview01'>1jef</scene>, resolution 1.77&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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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|GENE=
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}}
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'''TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JEF 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].
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1JEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEF OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299852 15299852]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15299852 15299852]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
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[[Category: inhibitor complex]]
[[Category: inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:02:17 2008''

Revision as of 10:02, 20 March 2008


PDB ID 1jef

Drag the structure with the mouse to rotate
, resolution 1.77Å
Ligands:
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3


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.

About this Structure

1JEF is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.

Reference

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

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