1n67: Difference between revisions
New page: left|200px<br /><applet load="1n67" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n67, resolution 1.90Å" /> '''Clumping Factor A fr... |
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[[Image:1n67.gif|left|200px]]<br /><applet load="1n67" size=" | [[Image:1n67.gif|left|200px]]<br /><applet load="1n67" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1n67, resolution 1.90Å" /> | caption="1n67, resolution 1.90Å" /> | ||
'''Clumping Factor A from Staphylococcus aureus'''<br /> | '''Clumping Factor A from Staphylococcus aureus'''<br /> | ||
==Overview== | ==Overview== | ||
We report here the crystal structure of the minimal ligand-binding segment | 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== | ||
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:// | 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.]] | ||
[[Category: Deivanayagam, C | [[Category: Deivanayagam, C C.S.]] | ||
[[Category: Hook, M.]] | [[Category: Hook, M.]] | ||
[[Category: Narayana, S | [[Category: Narayana, S V.L.]] | ||
[[Category: Rajashankar, K | [[Category: Rajashankar, K R.]] | ||
[[Category: Wann, E | [[Category: Wann, E R.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: clumping factor]] | [[Category: clumping factor]] | ||
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[[Category: staphylococcus aureus]] | [[Category: staphylococcus aureus]] | ||
''Page seeded by [http:// | ''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
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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 MG 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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