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1n67

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(New page: 200px<br /><applet load="1n67" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n67, resolution 1.90&Aring;" /> '''Clumping Factor A fr...)
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[[Image:1n67.gif|left|200px]]<br /><applet load="1n67" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n67.gif|left|200px]]<br /><applet load="1n67" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n67, resolution 1.90&Aring;" />
caption="1n67, resolution 1.90&Aring;" />
'''Clumping Factor A from Staphylococcus aureus'''<br />
'''Clumping Factor A from Staphylococcus aureus'''<br />
==Overview==
==Overview==
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We report here the crystal structure of the minimal ligand-binding segment, of the Staphylococcus aureus MSCRAMM, clumping factor A. This, fibrinogen-binding segment contains two similarly folded domains. The fold, observed is a new variant of the immunoglobulin motif that we have called, DE-variant or the DEv-IgG fold. This subgroup includes the ligand-binding, domain of the collagen-binding S.aureus MSCRAMM CNA, and many other, structures previously classified as jelly rolls. Structure predictions, suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so, far would also contain the same DEv-IgG fold. A systematic docking search, using the C-terminal region of the fibrinogen gamma-chain as a probe, suggested that a hydrophobic pocket formed between the two DEv-IgG domains, of the clumping factor as the ligand-binding site. Mutagenic substitution, of residues Tyr256, Pro336, Tyr338 and Lys389 in the clumping factor, which are proposed to contact the terminal residues (408)AGDV(411) of the, gamma-chain, resulted in proteins with no or markedly reduced affinity for, fibrinogen.
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We report here the crystal structure of the minimal ligand-binding segment of the Staphylococcus aureus MSCRAMM, clumping factor A. This fibrinogen-binding segment contains two similarly folded domains. The fold observed is a new variant of the immunoglobulin motif that we have called DE-variant or the DEv-IgG fold. This subgroup includes the ligand-binding domain of the collagen-binding S.aureus MSCRAMM CNA, and many other structures previously classified as jelly rolls. Structure predictions suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so far would also contain the same DEv-IgG fold. A systematic docking search using the C-terminal region of the fibrinogen gamma-chain as a probe suggested that a hydrophobic pocket formed between the two DEv-IgG domains of the clumping factor as the ligand-binding site. Mutagenic substitution of residues Tyr256, Pro336, Tyr338 and Lys389 in the clumping factor, which are proposed to contact the terminal residues (408)AGDV(411) of the gamma-chain, resulted in proteins with no or markedly reduced affinity for fibrinogen.
==About this Structure==
==About this Structure==
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1N67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N67 OCA].
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1N67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N67 OCA].
==Reference==
==Reference==
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[[Category: Carson, M.]]
[[Category: Carson, M.]]
[[Category: Chen, W.]]
[[Category: Chen, W.]]
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[[Category: Deivanayagam, C.C.S.]]
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[[Category: Deivanayagam, C C.S.]]
[[Category: Hook, M.]]
[[Category: Hook, M.]]
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[[Category: Narayana, S.V.L.]]
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[[Category: Narayana, S V.L.]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar, K R.]]
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[[Category: Wann, E.R.]]
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[[Category: Wann, E R.]]
[[Category: MG]]
[[Category: MG]]
[[Category: clumping factor]]
[[Category: clumping factor]]
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[[Category: staphylococcus aureus]]
[[Category: staphylococcus aureus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:59:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:39 2008''

Revision as of 12:02, 21 February 2008


1n67, resolution 1.90Å

Drag the structure with the mouse to rotate

Clumping Factor A from Staphylococcus aureus

Overview

We report here the crystal structure of the minimal ligand-binding segment of the Staphylococcus aureus MSCRAMM, clumping factor A. This fibrinogen-binding segment contains two similarly folded domains. The fold observed is a new variant of the immunoglobulin motif that we have called DE-variant or the DEv-IgG fold. This subgroup includes the ligand-binding domain of the collagen-binding S.aureus MSCRAMM CNA, and many other structures previously classified as jelly rolls. Structure predictions suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so far would also contain the same DEv-IgG fold. A systematic docking search using the C-terminal region of the fibrinogen gamma-chain as a probe suggested that a hydrophobic pocket formed between the two DEv-IgG domains of the clumping factor as the ligand-binding site. Mutagenic substitution of residues Tyr256, Pro336, Tyr338 and Lys389 in the clumping factor, which are proposed to contact the terminal residues (408)AGDV(411) of the gamma-chain, resulted in proteins with no or markedly reduced affinity for fibrinogen.

About this Structure

1N67 is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.

Reference

A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A., Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, Hook M, Narayana SV, EMBO J. 2002 Dec 16;21(24):6660-72. PMID:12485987

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