4bl4: Difference between revisions

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'''Unreleased structure'''


The entry 4bl4 is ON HOLD  until Paper Publication
==Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.==
<StructureSection load='4bl4' size='340' side='right'caption='[[4bl4]], [[Resolution|resolution]] 4.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bl4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_ZS7 Borreliella burgdorferi ZS7]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4atr 4atr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BL4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.06&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bl4 OCA], [https://pdbe.org/4bl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bl4 RCSB], [https://www.ebi.ac.uk/pdbsum/4bl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bl4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3BZN5_BORBZ A0A0H3BZN5_BORBZ]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.


Authors: Caesar, J.J.E., Wallich, R., Kraiczy, P., Zipfel, P.F., Lea, S.M.
Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.,Caesar JJ, Wallich R, Kraiczy P, Zipfel PF, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):629-33. doi: , 10.1107/S1744309113012748. Epub 2013 May 23. PMID:23722839<ref>PMID:23722839</ref>


Description: Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bl4" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Complement Regulator-Acquiring Surface Protein|Complement Regulator-Acquiring Surface Protein]]
*[[Complement regulator-acquiring surface protein|Complement regulator-acquiring surface protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi ZS7]]
[[Category: Large Structures]]
[[Category: Caesar JJE]]
[[Category: Kraiczy P]]
[[Category: Lea SM]]
[[Category: Wallich R]]
[[Category: Zipfel PF]]

Latest revision as of 11:53, 20 December 2023

Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.

4bl4, resolution 4.06Å

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