1d2p: Difference between revisions
New page: left|200px<br /><applet load="1d2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2p, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1d2p.jpg|left|200px]]<br /><applet load="1d2p" size=" | [[Image:1d2p.jpg|left|200px]]<br /><applet load="1d2p" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1d2p, resolution 2.50Å" /> | caption="1d2p, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF TWO B REPEAT UNITS (B1B2) OF THE COLLAGEN BINDING PROTEIN (CNA) OF STAPHYLOCOCCUS AUREUS'''<br /> | '''CRYSTAL STRUCTURE OF TWO B REPEAT UNITS (B1B2) OF THE COLLAGEN BINDING PROTEIN (CNA) OF STAPHYLOCOCCUS AUREUS'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGORUND: The Staphylococcus aureus collagen-binding protein Cna | BACKGORUND: The Staphylococcus aureus collagen-binding protein Cna mediates bacterial adherence to collagen. The primary sequence of Cna has a non-repetitive collagen-binding A region, followed by the repetitive B region. The B region has one to four 23 kDa repeat units (B(1)-B(4)), depending on the strain of origin. The affinity of the A region for collagen is independent of the B region. However, the B repeat units have been suggested to serve as a 'stalk' that projects the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. To understand the biological role of these B-region repeats we determined their three-dimensional structure. RESULTS: B(1) has two domains (D(1) and D(2)) placed side-by-side. D(1) and D(2) have similar secondary structure and exhibit a unique fold that resembles but is the inverse of the immunoglobulin-like (IgG-like) domains. Comparison with similar immunoglobulin superfamily (IgSF) structures shows novel packing arrangements between the D(1) and D(2) domains. In the B(1)B(2) crystal structure, an omission of a single glycine residue in the D(2)-D(3) linker loop, compared to the D(1)-D(2) and D(3)-D(4) linker loops, resulted in projection of the D(3) and D(4) in a spatially new orientation. We also present a model for B(1)B(2)B(3)B(4). CONCLUSIONS: The B region of the Cna collagen adhesin has a novel fold that is reminiscent of but is inverse in nature to the IgG fold. This B region assembly could effectively provide the needed flexibility and stability for presenting the ligand binding A region away from the bacterial cell surface. | ||
==About this Structure== | ==About this Structure== | ||
1D2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http:// | 1D2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2P OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Deivanayagam, C | [[Category: Deivanayagam, C C.S.]] | ||
[[Category: Hook, M.]] | [[Category: Hook, M.]] | ||
[[Category: Narayana, S | [[Category: Narayana, S V.L.]] | ||
[[Category: Rich, R | [[Category: Rich, R L.]] | ||
[[Category: cna]] | [[Category: cna]] | ||
[[Category: collagen]] | [[Category: collagen]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:29 2008'' | ||
Revision as of 13:12, 21 February 2008
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CRYSTAL STRUCTURE OF TWO B REPEAT UNITS (B1B2) OF THE COLLAGEN BINDING PROTEIN (CNA) OF STAPHYLOCOCCUS AUREUS
OverviewOverview
BACKGORUND: The Staphylococcus aureus collagen-binding protein Cna mediates bacterial adherence to collagen. The primary sequence of Cna has a non-repetitive collagen-binding A region, followed by the repetitive B region. The B region has one to four 23 kDa repeat units (B(1)-B(4)), depending on the strain of origin. The affinity of the A region for collagen is independent of the B region. However, the B repeat units have been suggested to serve as a 'stalk' that projects the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. To understand the biological role of these B-region repeats we determined their three-dimensional structure. RESULTS: B(1) has two domains (D(1) and D(2)) placed side-by-side. D(1) and D(2) have similar secondary structure and exhibit a unique fold that resembles but is the inverse of the immunoglobulin-like (IgG-like) domains. Comparison with similar immunoglobulin superfamily (IgSF) structures shows novel packing arrangements between the D(1) and D(2) domains. In the B(1)B(2) crystal structure, an omission of a single glycine residue in the D(2)-D(3) linker loop, compared to the D(1)-D(2) and D(3)-D(4) linker loops, resulted in projection of the D(3) and D(4) in a spatially new orientation. We also present a model for B(1)B(2)B(3)B(4). CONCLUSIONS: The B region of the Cna collagen adhesin has a novel fold that is reminiscent of but is inverse in nature to the IgG fold. This B region assembly could effectively provide the needed flexibility and stability for presenting the ligand binding A region away from the bacterial cell surface.
About this StructureAbout this Structure
1D2P is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Novel fold and assembly of the repetitive B region of the Staphylococcus aureus collagen-binding surface protein., Deivanayagam CC, Rich RL, Carson M, Owens RT, Danthuluri S, Bice T, Hook M, Narayana SV, Structure. 2000 Jan 15;8(1):67-78. PMID:10673425
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