132l
From Proteopedia
(New page: 200px<br /><applet load="132l" size="450" color="white" frame="true" align="right" spinBox="true" caption="132l, resolution 1.8Å" /> '''STRUCTURAL CONSEQUENC...) |
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| - | [[Image:132l.gif|left|200px]]<br /><applet load="132l" size=" | + | [[Image:132l.gif|left|200px]]<br /><applet load="132l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="132l, resolution 1.8Å" /> | caption="132l, resolution 1.8Å" /> | ||
'''STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chemical modification of proteins has been and continues to be an | + | Chemical modification of proteins has been and continues to be an important biochemical tool for the study of protein structure and function. One such type of approach has been the reductive methylation of lysine residues. In order to address the consequences of such methylation on the crystallization and structural properties of a protein, the three-dimensional structure of hen egg white lysozyme in which all lysine residues have been alkylated has been determined and refined to a nominal resolution of 1.8 A and a crystallographic R factor of 17.3%. Crystals used in the investigation were grown from 1.5-1.8 M MgSO4 and 50 mM Tris at pH 8.0 and belonged to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 30.6 A, b = 56.3 A, c = 73.2 A, and one molecule per asymmetric unit. It was not possible to grow crystals of the modified lysozyme under the conditions normally employed for the hen egg white protein. Overall, the three-dimensional structures of the native lysozyme and the modified protein are very similar with only two surface loops differing to any significant extent. Specifically, the positions of the alpha-carbons for these two forms of the protein, excluding the surface loops, superimpose with a root-mean-square value of 0.40 A. The magnitude of the structural changes observed between the modified an unmodified forms of lysozyme is similar to that seen when an identical protein structure is solved in two different crystalline lattices.(ABSTRACT TRUNCATED AT 250 WORDS) |
==About this Structure== | ==About this Structure== | ||
| - | 132L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with DML 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:// | + | 132L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=DML:'>DML</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=132L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Rypniewski, W | + | [[Category: Rypniewski, W R.]] |
[[Category: DML]] | [[Category: DML]] | ||
[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:37:59 2008'' |
Revision as of 09:38, 21 February 2008
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STRUCTURAL CONSEQUENCES OF REDUCTIVE METHYLATION OF LYSINE RESIDUES IN HEN EGG WHITE LYSOZYME: AN X-RAY ANALYSIS AT 1.8 ANGSTROMS RESOLUTION
Overview
Chemical modification of proteins has been and continues to be an important biochemical tool for the study of protein structure and function. One such type of approach has been the reductive methylation of lysine residues. In order to address the consequences of such methylation on the crystallization and structural properties of a protein, the three-dimensional structure of hen egg white lysozyme in which all lysine residues have been alkylated has been determined and refined to a nominal resolution of 1.8 A and a crystallographic R factor of 17.3%. Crystals used in the investigation were grown from 1.5-1.8 M MgSO4 and 50 mM Tris at pH 8.0 and belonged to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 30.6 A, b = 56.3 A, c = 73.2 A, and one molecule per asymmetric unit. It was not possible to grow crystals of the modified lysozyme under the conditions normally employed for the hen egg white protein. Overall, the three-dimensional structures of the native lysozyme and the modified protein are very similar with only two surface loops differing to any significant extent. Specifically, the positions of the alpha-carbons for these two forms of the protein, excluding the surface loops, superimpose with a root-mean-square value of 0.40 A. The magnitude of the structural changes observed between the modified an unmodified forms of lysozyme is similar to that seen when an identical protein structure is solved in two different crystalline lattices.(ABSTRACT TRUNCATED AT 250 WORDS)
About this Structure
132L is a Single protein structure of sequence from [1] with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8-A resolution., Rypniewski WR, Holden HM, Rayment I, Biochemistry. 1993 Sep 21;32(37):9851-8. PMID:8373783
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