1mi0: Difference between revisions

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<StructureSection load='1mi0' size='340' side='right'caption='[[1mi0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1mi0' size='340' side='right'caption='[[1mi0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mi0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Finm2 Finm2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mi0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI0 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mhx|1mhx]]</div></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]] 1.85&#8491;</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=1mi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi0 OCA], [https://pdbe.org/1mi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi0 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=1mi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi0 OCA], [https://pdbe.org/1mi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q53291_FINMA Q53291_FINMA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mi0 ConSurf].
</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=1mi0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We recently described two protein G variants (NuG1 and NuG2) with redesigned first hairpins that were almost twice as stable, folded 100-fold faster, and had a switched folding mechanism relative to the wild-type protein. To test the structural accuracy of our design algorithm and to provide insights to the dramatic changes in the kinetics and thermodynamics of folding, we have now determined the crystal structures of NuG1 and NuG2 to 1.8 A and 1.85 A, respectively. We find that they adopt hairpin structures that are closer to the computational models than to wild-type protein G; the RMSD of the NuG1 hairpin to the design model and the wild-type structure are 1.7 A and 5.1 A, respectively. The crystallographic B factor in the redesigned first hairpin of NuG1 is systematically higher than the second hairpin, suggesting that the redesigned region is somewhat less rigid. A second round of structure-based design yielded new variants of NuG1 and NuG2, which are further stabilized by 0.5 kcal/mole and 0.9 kcal/mole.
Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2.,Nauli S, Kuhlman B, Le Trong I, Stenkamp RE, Teller D, Baker D Protein Sci. 2002 Dec;11(12):2924-31. PMID:12441390<ref>PMID:12441390</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mi0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Protein G|Protein G]]
*[[Protein G|Protein G]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Finm2]]
[[Category: Finegoldia magna ATCC 29328]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baker, D]]
[[Category: Baker D]]
[[Category: Kuhlman, B]]
[[Category: Kuhlman B]]
[[Category: Nauli, S]]
[[Category: Le Trong I]]
[[Category: Stenkamp, R E]]
[[Category: Nauli S]]
[[Category: Teller, D C]]
[[Category: Stenkamp RE]]
[[Category: Trong, I Le]]
[[Category: Teller DC]]
[[Category: Alpha-beta protein]]
[[Category: Immune system]]
[[Category: Redesigned beta-hairpin]]

Latest revision as of 10:44, 14 February 2024

Crystal Structure of the redesigned protein G variant NuG2Crystal Structure of the redesigned protein G variant NuG2

Structural highlights

1mi0 is a 2 chain structure with sequence from Finegoldia magna ATCC 29328. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q53291_FINMA

Evolutionary Conservation

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

See Also

1mi0, resolution 1.85Å

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OCA
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