1d2p

<table><tr><td colspan='2'>[[1d2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D2P FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d2o|1d2o]], [[1amx|1amx]]</div></td></tr>

[[https://www.uniprot.org/uniprot/CNA_STAAU CNA_STAAU]] Mediates attachment of staphylococcal cells to collagen-containing substrata.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10673425</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Deivanayagam, C C.S]]

[[Category: Hook, M]]

[[Category: Narayana, S V.L]]

[[Category: Rich, R L]]

[[Category: Cna]]

[[Category: Collagen]]

[[Category: Igg]]

[[Category: Igsf]]

[[Category: Mscramm]]

[[Category: Structural protein]]