2g8c: Difference between revisions

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<StructureSection load='2g8c' size='340' side='right'caption='[[2g8c]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='2g8c' size='340' side='right'caption='[[2g8c]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2g8c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G8C FirstGlance]. <br>
<table><tr><td colspan='2'>[[2g8c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G8C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=2g8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g8c OCA], [https://pdbe.org/2g8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g8c RCSB], [https://www.ebi.ac.uk/pdbsum/2g8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g8c ProSAT]</span></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=2g8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g8c OCA], [https://pdbe.org/2g8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g8c RCSB], [https://www.ebi.ac.uk/pdbsum/2g8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g8c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35210]]
[[Category: Borreliella burgdorferi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Koide, S]]
[[Category: Koide S]]
[[Category: Makabe, K]]
[[Category: Makabe K]]
[[Category: Tereshko, V]]
[[Category: Tereshko V]]
[[Category: Beta sheet]]
[[Category: Lipid binding protein]]

Latest revision as of 12:36, 30 August 2023

Atomic-resolution crystal structure of Borrelia burgdorferi OspA via surface entropy reductionAtomic-resolution crystal structure of Borrelia burgdorferi OspA via surface entropy reduction

Structural highlights

2g8c is a 1 chain structure with sequence from Borreliella burgdorferi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OSPA_BORBU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Outer surface protein A (OspA) from Borrelia burgdorferi has an unusual dumbbell-shaped structure in which two globular domains are connected with a "single-layer" beta-sheet (SLB). The protein is highly soluble, and it has been recalcitrant to crystallization. Only OspA complexes with Fab fragments have been successfully crystallized. OspA contains a large number of Lys and Glu residues, and these "high entropy" residues may disfavor crystal packing because some of them would need to be immobilized in forming a crystal lattice. We rationally designed a total of 13 surface mutations in which Lys and Glu residues were replaced with Ala or Ser. We successfully crystallized the mutant OspA without a bound Fab fragment and extended structure analysis to a 1.15 Angstroms resolution. The new high-resolution structure revealed a unique backbone hydration pattern of the SLB segment in which water molecules fill the "weak spots" on both faces of the antiparallel beta-sheet. These well-defined water molecules provide additional structural links between adjacent beta-strands, and thus they may be important for maintaining the rigidity of the SLB that inherently lacks tight packing afforded by a hydrophobic core. The structure also revealed new information on the side-chain dynamics and on a solvent-accessible cavity in the core of the C-terminal globular domain. This work demonstrates the utility of extensive surface mutation in crystallizing recalcitrant proteins and dramatically improving the resolution of crystal structures, and provides new insights into the stabilization mechanism of OspA.

Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering.,Makabe K, Tereshko V, Gawlak G, Yan S, Koide S Protein Sci. 2006 Aug;15(8):1907-14. Epub 2006 Jul 5. PMID:16823038[1]

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

See Also

References

  1. Makabe K, Tereshko V, Gawlak G, Yan S, Koide S. Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering. Protein Sci. 2006 Aug;15(8):1907-14. Epub 2006 Jul 5. PMID:16823038 doi:10.1110/ps.062246706

2g8c, resolution 1.15Å

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