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2y3f

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Revision as of 02:25, 5 August 2016

TRAPTAVIDIN, BIOTIN BOUND FORM

Structural highlights

2y3f is a 1 chain structure with sequence from As 4.1583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1swh, 2bc3, 1vwq, 1swf, 1sre, 1lcw, 2rtb, 1swp, 1hxz, 1rxj, 1swe, 1mm9, 2rtr, 1swa, 2rto, 2rtd, 1stp, 1n43, 1sri, 2izh, 1slf, 1swc, 1vwr, 1swl, 1ndj, 1str, 1vwm, 1slg, 1swd, 1swq, 1swu, 2y3e, 1i9h, 2rtj, 1swj, 2rtl, 2iza, 1vwk, 1vwn, 1vwg, 1moy, 1sts, 1hqq, 1vwi, 2izg, 2izb, 1swg, 1luq, 1swk, 2izk, 1sws, 1n4j, 2izd, 1swt, 1lcv, 1df8, 1vwl, 2wpu, 1vwb, 1srj, 2rtk, 1kl3, 2rti, 2izf, 1swr, 2rth, 2rtm, 2izi, 1vwf, 1vwh, 1pts, 1mk5, 1hxl, 2f01, 1vwd, 1nc9, 1sle, 1vwj, 2ize, 2rtf, 2rtp, 1n9y, 1n9m, 1lcz, 1hy2, 1nqm, 1vwa, 2izl, 2izc, 1kl5, 1mep, 1sld, 1rxh, 1vwc, 1rsu, 1nbx, 2izj, 1srh, 1rst, 1kff, 1srg, 1vwe, 2rtg, 1srf, 1kl4, 1rxk, 2rtq, 2rte, 1swb, 1vwo, 2rta, 2rtc, 1swo, 2rtn, 1swn, 1n7y, 1vwp
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

Publication Abstract from PubMed

The interaction between streptavidin and biotin is one of the strongest non-covalent interactions in nature. Streptavidin is a widely used tool and a paradigm for protein-ligand interactions. We recently developed a streptavidin mutant, termed traptavidin, possessing 10-fold lower off-rate for biotin, with increased mechanical and thermal stability. Here, we determined crystal structures of apo-traptavidin and biotin-traptavidin at 1.5 A resolution. In apo-streptavidin the L3/4 loop, near biotin's valeryl tail, is typically disordered and open, but closes upon biotin binding. In contrast, this L3/4 loop was shut in both apo-traptavidin and biotin-traptavidin. The reduced flexibility of L3/4 and decreased conformational change on biotin binding provide an explanation for traptavidin's reduced biotin off-rate and on-rate. The L3/4 loop includes Ser-45, which forms a hydrogen bond to biotin consistently in traptavidin but erratically in streptavidin. Reduced breakage of the biotin:Ser-45 hydrogen bond in traptavidin is likely to inhibit the initiating event in biotin's dissociation pathway. We generated a traptavidin with 1 biotin binding site rather than 4, which showed a similarly slow off-rate, demonstrating that traptavidin's slow off-rate was governed by intra-subunit effects. Understanding the structural features of this tenacious interaction may assist design of even stronger affinity tags and inhibitors.

How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimeric tetramer.,Chivers CE, Koner AL, Lowe ED, Howarth M Biochem J. 2011 Jan 18. PMID:21241253^[1]

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

References

↑ Chivers CE, Koner AL, Lowe ED, Howarth M. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimeric tetramer. Biochem J. 2011 Jan 18. PMID:21241253 doi:10.1042/BJ20101593

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/2y3f"

@@ Line 1: / Line 1: @@
 ==TRAPTAVIDIN, BIOTIN BOUND FORM==
 <StructureSection load='2y3f' size='340' side='right' caption='[[2y3f]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3F FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1swh|1swh]], [[2bc3|2bc3]], [[1vwq|1vwq]], [[1swf|1swf]], [[1sre|1sre]], [[1lcw|1lcw]], [[2rtb|2rtb]], [[1swp|1swp]], [[1hxz|1hxz]], [[1rxj|1rxj]], [[1swe|1swe]], [[1mm9|1mm9]], [[2rtr|2rtr]], [[1swa|1swa]], [[2rto|2rto]], [[2rtd|2rtd]], [[1stp|1stp]], [[1n43|1n43]], [[1sri|1sri]], [[2izh|2izh]], [[1slf|1slf]], [[1swc|1swc]], [[1vwr|1vwr]], [[1swl|1swl]], [[1ndj|1ndj]], [[1str|1str]], [[1vwm|1vwm]], [[1slg|1slg]], [[1swd|1swd]], [[1swq|1swq]], [[1swu|1swu]], [[2y3e|2y3e]], [[1i9h|1i9h]], [[2rtj|2rtj]], [[1swj|1swj]], [[2rtl|2rtl]], [[2iza|2iza]], [[1vwk|1vwk]], [[1vwn|1vwn]], [[1vwg|1vwg]], [[1moy|1moy]], [[1sts|1sts]], [[1hqq|1hqq]], [[1vwi|1vwi]], [[2izg|2izg]], [[2izb|2izb]], [[1swg|1swg]], [[1luq|1luq]], [[1swk|1swk]], [[2izk|2izk]], [[1sws|1sws]], [[1n4j|1n4j]], [[2izd|2izd]], [[1swt|1swt]], [[1lcv|1lcv]], [[1df8|1df8]], [[1vwl|1vwl]], [[2wpu|2wpu]], [[1vwb|1vwb]], [[1srj|1srj]], [[2rtk|2rtk]], [[1kl3|1kl3]], [[2rti|2rti]], [[2izf|2izf]], [[1swr|1swr]], [[2rth|2rth]], [[2rtm|2rtm]], [[2izi|2izi]], [[1vwf|1vwf]], [[1vwh|1vwh]], [[1pts|1pts]], [[1mk5|1mk5]], [[1hxl|1hxl]], [[2f01|2f01]], [[1vwd|1vwd]], [[1nc9|1nc9]], [[1sle|1sle]], [[1vwj|1vwj]], [[2ize|2ize]], [[2rtf|2rtf]], [[2rtp|2rtp]], [[1n9y|1n9y]], [[1n9m|1n9m]], [[1lcz|1lcz]], [[1hy2|1hy2]], [[1nqm|1nqm]], [[1vwa|1vwa]], [[2izl|2izl]], [[2izc|2izc]], [[1kl5|1kl5]], [[1mep|1mep]], [[1sld|1sld]], [[1rxh|1rxh]], [[1vwc|1vwc]], [[1rsu|1rsu]], [[1nbx|1nbx]], [[2izj|2izj]], [[1srh|1srh]], [[1rst|1rst]], [[1kff|1kff]], [[1srg|1srg]], [[1vwe|1vwe]], [[2rtg|2rtg]], [[1srf|1srf]], [[1kl4|1kl4]], [[1rxk|1rxk]], [[2rtq|2rtq]], [[2rte|2rte]], [[1swb|1swb]], [[1vwo|1vwo]], [[2rta|2rta]], [[2rtc|2rtc]], [[1swo|1swo]], [[2rtn|2rtn]], [[1swn|1swn]], [[1n7y|1n7y]], [[1vwp|1vwp]]</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=2y3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3f RCSB], [http://www.ebi.ac.uk/pdbsum/2y3f PDBsum]</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=2y3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3f OCA], [http://pdbe.org/2y3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3f RCSB], [http://www.ebi.ac.uk/pdbsum/2y3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2y3f" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 24: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Streptomyces avidinii]]
+[[Category: As 4 1583]]
 [[Category: Chivers, C E]]
 [[Category: Howarth, M]]

2y3f

From Proteopedia

Revision as of 02:25, 5 August 2016

TRAPTAVIDIN, BIOTIN BOUND FORM

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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