5cf3: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal structures of Bbp from Staphylococcus aureus==

== Structural highlights ==

<table><tr><td colspan='2'>[[5cf3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CF3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cfa|5cfa]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cf3 OCA], [http://pdbe.org/5cf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cf3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cf3 PDBsum]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/BBP_STAAU BBP_STAAU]] Specifically interacts with bone sialoprotein (BSP), a glycoprotein of bone and dentin extracellular matrix. Could contribute to staphylococcal osteomyelitis and arthritis.<ref>PMID:10642520</ref>

== Publication Abstract from PubMed ==

Bone sialoprotein-binding protein (Bbp), a MSCRAMMs (Microbial Surface Components Recognizing Adhesive Matrix Molecules) family protein expressed on the surface of Staphylococcus aureus (S. aureus), mediates adherence to fibrinogen alpha (Fg alpha), a component in the extracellular matrix of the host cell and is important for infection and pathogenesis. In this study, we solved the crystal structures of apo-Bbp(273-598) and Bbp(273-598)-Fg alpha(561-575) complex at a resolution of 2.03 A and 1.45 A, respectively. Apo-Bbp(273-598) contained the ligand binding region N2 and N3 domains, both of which followed a DE variant IgG fold characterized by an additional D1 strand in N2 domain and D1' and D2' strands in N3 domain. The peptide mapped to the Fg alpha(561-575) bond to Bbp(273-598) on the open groove between the N2 and N3 domains. Strikingly, the disordered C-terminus in the apo-form reorganized into a highly-ordered loop and a beta-strand G'' covering the ligand upon ligand binding. Bbp(Ala298-Gly301) in the N2 domain of the Bbp(273-598)-Fg alpha(561-575) complex, which is a loop in the apo-form, formed a short alpha-helix to interact tightly with the peptide. In addition, Bbp(Ser547-Gln561) in the N3 domain moved toward the binding groove to make contact directly with the peptide, while Bbp(Asp338-Gly355) and Bbp(Thr365-Tyr387) in N2 domain shifted their configurations to stabilize the reorganized C-terminus mainly through strong hydrogen bonds. Altogether, our results revealed the molecular basis for Bbp-ligand interaction and advanced our understanding of S. aureus infection process.

~~The entry 5cf3 is ON HOLD until Paper Publication~~

Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen alpha.,Zhang X, Wu M, Zhuo W, Gu J, Zhang S, Ge J, Yang M Protein Cell. 2015 Oct;6(10):757-66. doi: 10.1007/s13238-015-0205-x. Epub 2015, Sep 8. PMID:26349459<ref>PMID:26349459</ref>

~~Authors: Yu~~, Y.~~, Zhang, X~~.~~Y., Gu, J.K~~.

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

</div>

~~Description~~: ~~Crystal structures of Bbp from Staphylococcus aureus~~

~~[[Category: Unreleased Structures]]~~

== References ==

[[Category: Gu, J.K]]

~~[[Category: Zhang, X.Y~~]]

__TOC__

</StructureSection>

[[Category: Gu, J K]]

[[Category: Yu, Y]]

[[Category: Zhang, X Y]]

[[Category: Bbp]]

[[Category: Fibrinogen]]

[[Category: Mscramm]]

[[Category: Protein binding]]

[[Category: Sdr]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structures of Bbp from Staphylococcus aureus==
+<StructureSection load='5cf3' size='340' side='right' caption='[[5cf3]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5cf3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CF3 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cfa|5cfa]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cf3 OCA], [http://pdbe.org/5cf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cf3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cf3 PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BBP_STAAU BBP_STAAU]] Specifically interacts with bone sialoprotein (BSP), a glycoprotein of bone and dentin extracellular matrix. Could contribute to staphylococcal osteomyelitis and arthritis.<ref>PMID:10642520</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bone sialoprotein-binding protein (Bbp), a MSCRAMMs (Microbial Surface Components Recognizing Adhesive Matrix Molecules) family protein expressed on the surface of Staphylococcus aureus (S. aureus), mediates adherence to fibrinogen alpha (Fg alpha), a component in the extracellular matrix of the host cell and is important for infection and pathogenesis. In this study, we solved the crystal structures of apo-Bbp(273-598) and Bbp(273-598)-Fg alpha(561-575) complex at a resolution of 2.03 A and 1.45 A, respectively. Apo-Bbp(273-598) contained the ligand binding region N2 and N3 domains, both of which followed a DE variant IgG fold characterized by an additional D1 strand in N2 domain and D1' and D2' strands in N3 domain. The peptide mapped to the Fg alpha(561-575) bond to Bbp(273-598) on the open groove between the N2 and N3 domains. Strikingly, the disordered C-terminus in the apo-form reorganized into a highly-ordered loop and a beta-strand G'' covering the ligand upon ligand binding. Bbp(Ala298-Gly301) in the N2 domain of the Bbp(273-598)-Fg alpha(561-575) complex, which is a loop in the apo-form, formed a short alpha-helix to interact tightly with the peptide. In addition, Bbp(Ser547-Gln561) in the N3 domain moved toward the binding groove to make contact directly with the peptide, while Bbp(Asp338-Gly355) and Bbp(Thr365-Tyr387) in N2 domain shifted their configurations to stabilize the reorganized C-terminus mainly through strong hydrogen bonds. Altogether, our results revealed the molecular basis for Bbp-ligand interaction and advanced our understanding of S. aureus infection process.
-The entry 5cf3 is ON HOLD  until Paper Publication
+Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen alpha.,Zhang X, Wu M, Zhuo W, Gu J, Zhang S, Ge J, Yang M Protein Cell. 2015 Oct;6(10):757-66. doi: 10.1007/s13238-015-0205-x. Epub 2015, Sep 8. PMID:26349459<ref>PMID:26349459</ref>
-Authors: Yu, Y., Zhang, X.Y., Gu, J.K.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structures of Bbp from Staphylococcus aureus
+<div class="pdbe-citations 5cf3" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Gu, J.K]]
+<references/>
-[[Category: Zhang, X.Y]]
+__TOC__
+</StructureSection>
+[[Category: Gu, J K]]
 [[Category: Yu, Y]]
+[[Category: Zhang, X Y]]
+[[Category: Bbp]]
+[[Category: Fibrinogen]]
+[[Category: Mscramm]]
+[[Category: Protein binding]]
+[[Category: Sdr]]