1em7
From Proteopedia
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==HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G== | ==HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G== | ||
| - | <StructureSection load='1em7' size='340' side='right' caption='[[1em7]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1em7' size='340' side='right'caption='[[1em7]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1em7]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1em7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EM7 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1em7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1em7 OCA], [https://pdbe.org/1em7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1em7 RCSB], [https://www.ebi.ac.uk/pdbsum/1em7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1em7 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. |
== 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=1em7 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=1em7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions. | ||
| - | + | ==See Also== | |
| - | + | *[[Protein G|Protein G]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Streptococcus sp]] |
| - | [[Category: | + | [[Category: Marinescu AM]] |
| - | [[Category: | + | [[Category: Mayo SL]] |
| - | [[Category: | + | [[Category: Strop P]] |
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Current revision
HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G
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