6t1g: Difference between revisions

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<StructureSection load='6t1g' size='340' side='right'caption='[[6t1g]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6t1g' size='340' side='right'caption='[[6t1g]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6t1g]] is a 2 chain structure with sequence from [https://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=6T1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T1G FirstGlance]. <br>
<table><tr><td colspan='2'>[[6t1g]] is a 2 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=6T1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T1G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HL9:5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-(1-pyridin-4-ylpiperidin-4-yl)pentanamide'>HL9</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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HL9:5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-(1-pyridin-4-ylpiperidin-4-yl)pentanamide'>HL9</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=6t1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1g OCA], [https://pdbe.org/6t1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t1g RCSB], [https://www.ebi.ac.uk/pdbsum/6t1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1g 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=6t1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1g OCA], [https://pdbe.org/6t1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t1g RCSB], [https://www.ebi.ac.uk/pdbsum/6t1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An artificial cofactor based on an organocatalyst embedded in a protein has been used to conduct the Baylis-Hillman reaction in a buffered system. As protein host, we chose streptavidin, as it can be easily crystallized and thereby supports the design process. The protein host around the cofactor was rationally designed on the basis of high-resolution crystal structures obtained after each variation of the amino acid sequence. Additionally, DFT-calculated intermediates and transition states were used to rationalize the observed activity. Finally, repeated cycles of structure determination and redesign led to a system with an up to one order of magnitude increase in activity over the bare cofactor and to the most active proteinogenic catalyst for the Baylis-Hillman reaction known today.
 
An Artificial Cofactor Catalyzing the Baylis-Hillman Reaction with Designed Streptavidin as Protein Host*.,Lechner H, Emann VR, Breuning M, Hocker B Chembiochem. 2021 Jan 5. doi: 10.1002/cbic.202000880. PMID:33400831<ref>PMID:33400831</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6t1g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1583]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hocker, B]]
[[Category: Streptomyces avidinii]]
[[Category: Lechner, H]]
[[Category: Hocker B]]
[[Category: Artificial cofactor]]
[[Category: Lechner H]]
[[Category: Biotin-binding protein]]
[[Category: Catalyst]]
[[Category: Streptavidin]]
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