146l: Difference between revisions

Revision as of 12:38, 21 February 2008

ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME

OverviewOverview

To understand better how the packing of side chains within the core influences protein structure and stability, the crystal structures were determined for eight variants of T4 lysozyme, each of which contains three to five substitutions at adjacent interior sites. Concerted main-chain and side-chain displacements, with movements of helical segments as large as 0.8 angstrom, were observed. In contrast, the angular conformations of the mutated side chains tended to remain unchanged, with torsion angles within 20 degrees of those in the wild-type structure. These observations suggest that not only the rotation of side chains but also movements of the main chain must be considered in the evaluation of which amino acid sequences are compatible with a given protein fold.

About this StructureAbout this Structure

146L is a Single protein structure of sequence from Enterobacteria phage t2 with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme., Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW, Science. 1993 Dec 10;262(5140):1715-8. PMID:8259514

Page seeded by OCA on Thu Feb 21 11:38:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:146l.gif|left|200px]]<br /><applet load="146l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:146l.gif|left|200px]]<br /><applet load="146l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="146l, resolution 1.85&Aring;" />
 '''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME'''<br />
 ==Overview==
-To understand better how the packing of side chains within the core, influences protein structure and stability, the crystal structures were, determined for eight variants of T4 lysozyme, each of which contains three, to five substitutions at adjacent interior sites. Concerted main-chain and, side-chain displacements, with movements of helical segments as large as, 0.8 angstrom, were observed. In contrast, the angular conformations of the, mutated side chains tended to remain unchanged, with torsion angles within, 20 degrees of those in the wild-type structure. These observations suggest, that not only the rotation of side chains but also movements of the main, chain must be considered in the evaluation of which amino acid sequences, are compatible with a given protein fold.
+To understand better how the packing of side chains within the core influences protein structure and stability, the crystal structures were determined for eight variants of T4 lysozyme, each of which contains three to five substitutions at adjacent interior sites. Concerted main-chain and side-chain displacements, with movements of helical segments as large as 0.8 angstrom, were observed. In contrast, the angular conformations of the mutated side chains tended to remain unchanged, with torsion angles within 20 degrees of those in the wild-type structure. These observations suggest that not only the rotation of side chains but also movements of the main chain must be considered in the evaluation of which amino acid sequences are compatible with a given protein fold.
 ==About this Structure==
-L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. 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=146L OCA].
+L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=146L OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Baldwin, E.]]
-[[Category: Matthews, B.W.]]
+[[Category: Matthews, B W.]]
 [[Category: BME]]
 [[Category: CL]]
 [[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:27:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:38:16 2008''