We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

3noc

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Designed ankyrin repeat protein (DARPin) binders to AcrB: Plasticity of the Interface

Structural highlights

3noc is a 5 chain structure with sequence from Escherichia coli K-12 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The formation of well-diffracting crystals is a major bottleneck in structural analysis of membrane proteins by X-ray crystallography. One approach to improve crystal quality is the use of DARPins as crystallization chaperones. Here, we present a detailed analysis of the interaction between DARPins and the integral membrane protein AcrB. We find that binders selected in vitro by ribosome display share a common epitope. The comparative analysis of three crystal structures of AcrB-DARPin complexes allowed us to study the plasticity of the interaction with this dominant binding site. Seemingly redundant AcrB-DARPin crystals show substantially different diffraction quality as a result of subtle differences in the binding geometry. This work exemplifies the importance to screen a number of crystallization chaperones to obtain optimal diffraction data. Crystallographic analysis is complemented by biophysical characterization of nine AcrB binders. We observe that small variations in the interface can lead to differing behavior of the DARPins with regards to affinity, stoichiometry of the complexes and specificity for their target.

Designed ankyrin repeat protein binders for the crystallization of AcrB: Plasticity of the dominant interface.,Monroe N, Sennhauser G, Seeger MA, Briand C, Grutter MG J Struct Biol. 2011 May;174(2):269-81. Epub 2011 Feb 4. PMID:21296164^[4]

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

References

↑ Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076
↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
↑ Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007
↑ Monroe N, Sennhauser G, Seeger MA, Briand C, Grutter MG. Designed ankyrin repeat protein binders for the crystallization of AcrB: Plasticity of the dominant interface. J Struct Biol. 2011 May;174(2):269-81. Epub 2011 Feb 4. PMID:21296164 doi:10.1016/j.jsb.2011.01.014

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3noc"

@@ Line 1: / Line 1: @@
 ==Designed ankyrin repeat protein (DARPin) binders to AcrB: Plasticity of the Interface==
-<StructureSection load='3noc' size='340' side='right' caption='[[3noc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='3noc' size='340' side='right'caption='[[3noc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3noc]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NOC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3noc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NOC FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</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]] 2.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j8s|2j8s]], [[3nog|3nog]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrB, acrE, b0462, JW0451 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3noc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3noc OCA], [https://pdbe.org/3noc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3noc RCSB], [https://www.ebi.ac.uk/pdbsum/3noc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3noc ProSAT]</span></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=3noc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3noc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3noc RCSB], [http://www.ebi.ac.uk/pdbsum/3noc PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3noc" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Ankyrin|Ankyrin]]
+*[[Ankyrin 3D structures|Ankyrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
 [[Category: Synthetic construct]]
-[[Category: Briand, C]]
+[[Category: Briand C]]
-[[Category: Gruetter, M G]]
+[[Category: Gruetter MG]]
-[[Category: Monroe, N]]
+[[Category: Monroe N]]
-[[Category: Crystallization chaperone]]
-[[Category: Designed ankyrin repeat protein]]
-[[Category: Drug-efflux pump]]
-[[Category: Membrane protein]]
-[[Category: Rnd]]
-[[Category: Transport protein]]
-[[Category: Transport protein-protein binding complex]]

3noc

From Proteopedia

Current revision

Designed ankyrin repeat protein (DARPin) binders to AcrB: Plasticity of the Interface

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox