2odm: Difference between revisions

Revision as of 19:17, 21 February 2008

Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape

OverviewOverview

The crystal structure of a conserved leucine rich protein, YlaN, from Staphylococcus aureus has been determined by X-ray crystallography to 2.3 A resolution. Whilst the precise function of S. aureus YlaN is unknown its homologue in B. subtilis has been shown to be essential for cell survival and is thought to be involved in controlling cell shape. The structure of S. aureus YlaN provides the first view of its protein family, which reveals that it is a novel homodimer whose subunit architecture is comprised of an antiparallel 3 helix bundle reminiscent of the helical arrangements seen in leucine zipper proteins. Analysis of the pattern of sequence conservation on the structure has led to the identification of two connected solvent exposed patches of conserved residues in each subunit located at one end of but on opposite faces of the molecule. We suggest that YlaN has a binding role in the cell rather than a catalytic function and a search for its ligand is underway to accelerate its exploitation as a target for antibiotic discovery.

About this StructureAbout this Structure

2ODM is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape., Xu L, Sedelnikova SE, Baker PJ, Hunt A, Errington J, Rice DW, Proteins. 2007 Aug 1;68(2):438-45. PMID:17469204

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OCA

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 ==Overview==
-The crystal structure of a conserved leucine rich protein, YlaN, from, Staphylococcus aureus has been determined by X-ray crystallography to 2.3, A resolution. Whilst the precise function of S. aureus YlaN is unknown its, homologue in B. subtilis has been shown to be essential for cell survival, and is thought to be involved in controlling cell shape. The structure of, S. aureus YlaN provides the first view of its protein family, which, reveals that it is a novel homodimer whose subunit architecture is, comprised of an antiparallel 3 helix bundle reminiscent of the helical, arrangements seen in leucine zipper proteins. Analysis of the pattern of, sequence conservation on the structure has led to the identification of, two connected solvent exposed patches of conserved residues in each, subunit located at one end of but on opposite faces of the molecule. We, suggest that YlaN has a binding role in the cell rather than a catalytic, function and a search for its ligand is underway to accelerate its, exploitation as a target for antibiotic discovery. Proteins 2007. (c) 2007, Wiley-Liss, Inc.
+The crystal structure of a conserved leucine rich protein, YlaN, from Staphylococcus aureus has been determined by X-ray crystallography to 2.3 A resolution. Whilst the precise function of S. aureus YlaN is unknown its homologue in B. subtilis has been shown to be essential for cell survival and is thought to be involved in controlling cell shape. The structure of S. aureus YlaN provides the first view of its protein family, which reveals that it is a novel homodimer whose subunit architecture is comprised of an antiparallel 3 helix bundle reminiscent of the helical arrangements seen in leucine zipper proteins. Analysis of the pattern of sequence conservation on the structure has led to the identification of two connected solvent exposed patches of conserved residues in each subunit located at one end of but on opposite faces of the molecule. We suggest that YlaN has a binding role in the cell rather than a catalytic function and a search for its ligand is underway to accelerate its exploitation as a target for antibiotic discovery.
 ==About this Structure==
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 ==Reference==
-Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape., Xu L, Sedelnikova SE, Baker PJ, Hunt A, Errington J, Rice DW, Proteins. 2007 Apr 27;68(2):438-445. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17469204 17469204]
+Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape., Xu L, Sedelnikova SE, Baker PJ, Hunt A, Errington J, Rice DW, Proteins. 2007 Aug 1;68(2):438-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17469204 17469204]
 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Baker, P.J.]]
+[[Category: Baker, P J.]]
 [[Category: Errington, J.]]
 [[Category: Hunt, A.]]
-[[Category: Rice, D.W.]]
+[[Category: Rice, D W.]]
-[[Category: Sedelnikova, S.E.]]
+[[Category: Sedelnikova, S E.]]
 [[Category: Xu, L.]]
 [[Category: triple helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:53:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:14 2008''