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1str

From Proteopedia

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[[Image:1str.gif|left|200px]]<br /><applet load="1str" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1str, resolution 1.80&Aring;" />
 
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'''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER'''<br />
 
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==Overview==
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==STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER==
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Recently, a cyclic peptide ligand, cyclo-Ac-[CHPQG-PPC]-NH2, that binds to streptavidin with high affinity was discovered by screening phage libraries. From the streptavidin-bound crystal structures of cyclo-Ac-[CHPQGPPC]-NH2 and of a related but more weakly binding linear ligand, FSHPQNT, we designed linear thiol-containing streptavidin binding ligands, FCH-PQNT-NH2 and Ac-CHPQNT-NH2, which are dimerized catalytically by the streptavidin crystal lattice of space group I222, as demonstrated by high performance liquid chromatography and mass spectrometry. The catalytic dimerization relies on presentation of the ligand thiols toward one another in the lattice. The streptavidin crystal lattice-mediated catalysis achieved by structure-based design is the first example of catalysis of a chemical reaction by a protein crystal lattice. The spontaneous and crystal catalyzed rates of disulfide formation were determined by high performance liquid chromatography at pH 3.1, 4.0, 5.0, and 6.0. The ratio of the catalyzed to uncatalyzed rate was maximal at pH 3.1 (kcat/kuncat = 3.8), diminishing to 1.2 at pH 6.0. The crystal structures of the streptavidin-bound dimerized peptide ligands, FCHPQNT-NH2 dimer at 1.95 A and Ac-CHPQNT-NH2 dimer at 1.80 A, are described and compared with the structures of streptavidin-bound FSHPQNT monomer and cyclo-Ac-[CHPQGPPC]-NH2 dimer.
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<StructureSection load='1str' size='340' side='right'caption='[[1str]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1str]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1STR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1str FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1str OCA], [https://pdbe.org/1str PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1str RCSB], [https://www.ebi.ac.uk/pdbsum/1str PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1str ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1str_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1str ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1STR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STR OCA].
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*[[Avidin 3D structures|Avidin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Topochemical catalysis achieved by structure-based ligand design., Katz BA, Cass RT, Liu B, Arze R, Collins N, J Biol Chem. 1995 Dec 29;270(52):31210-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8537386 8537386]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces avidinii]]
[[Category: Streptomyces avidinii]]
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[[Category: Arze, R.]]
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[[Category: Arze R]]
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[[Category: Cass, R T.]]
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[[Category: Cass RT]]
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[[Category: Collins, N.]]
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[[Category: Collins N]]
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[[Category: Katz, B A.]]
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[[Category: Katz BA]]
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[[Category: Liu, B.]]
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[[Category: Liu B]]
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[[Category: ACE]]
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[[Category: NH2]]
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[[Category: complex (glycoprotein/peptide)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:05 2008''
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Current revision

STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER

PDB ID 1str

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