3fil

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
+
==Structural and energetic determinants for hyperstable variants of GB1 obtained from in-vitro evolution==
-
[[Image:3fil.png|left|200px]]
+
<StructureSection load='3fil' size='340' side='right' caption='[[3fil]], [[Resolution|resolution]] 0.88&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3fil]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._'group_g' Streptococcus sp. 'group g']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FIL FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2on8|2on8]], [[2onq|2onq]], [[1pga|1pga]], [[1gb4|1gb4]], [[1fcc|1fcc]], [[2qmt|2qmt]]</td></tr>
 +
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1320 Streptococcus sp. 'group G'])</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fil OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fil RCSB], [http://www.ebi.ac.uk/pdbsum/3fil PDBsum]</span></td></tr>
 +
<table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/3fil_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
In previous work, a strongly stabilized variant of the beta1 domain of streptococcal protein G (Gbeta1) was obtained by an in vitro selection method. This variant, termed Gbeta1-M2, contains the four substitutions E15V, T16L, T18I, and N37L. Here we elucidated the molecular basis of the observed strong stabilizations. The contributions of these four residues were analyzed individually and in various combinations, additional selections with focused Gbeta1 gene libraries were performed, and the crystal structure of Gbeta1-M2 was determined. All single substitutions (E15V, T16L, T18I, and N37L) stabilize wild-type Gbeta1 by contributions of between 1.6 and 6.0 kJ mol(-1) (at 70 degrees C). Hydrophobic residues at positions 16 and 37 provide the major contribution to stabilization by enlarging the hydrophobic core of Gbeta1. They also increase the tendency to form dimers, as shown by dependence on the concentration of apparent molecular mass in analytical ultracentrifugation, by concentration-dependent stability, and by a strongly increased van't Hoff enthalpy of unfolding. The 0.88-A crystal structure of Gbeta1-M2 and NMR measurements in solution provide the explanation for the observed dimer formation. It involves a head-to-head arrangement of two Gbeta1-M2 molecules via six intermolecular hydrogen bonds between the two beta strands 2 and 2' and an adjacent self-complementary hydrophobic surface area, which is created by the T16L and N37L substitutions and a large 120 degrees rotation of the Tyr33 side chain. This removal of hydrophilic groups and the malleability of the created hydrophobic surface provide the basis for the dimer formation of stabilized Gbeta1 variants.
-
<!--
+
Dimer formation of a stabilized Gbeta1 variant: a structural and energetic analysis.,Thoms S, Max KE, Wunderlich M, Jacso T, Lilie H, Reif B, Heinemann U, Schmid FX J Mol Biol. 2009 Sep 4;391(5):918-32. Epub 2009 Jun 13. PMID:19527728<ref>PMID:19527728</ref>
-
The line below this paragraph, containing "STRUCTURE_3fil", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_3fil| PDB=3fil | SCENE= }}
+
-
===Structural and energetic determinants for hyperstable variants of GB1 obtained from in-vitro evolution===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_19527728}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 19527728 is the PubMed ID number.
+
</StructureSection>
-
-->
+
[[Category: Streptococcus sp. 'group g']]
-
{{ABSTRACT_PUBMED_19527728}}
+
-
 
+
-
==About this Structure==
+
-
3FIL is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIL OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:19527728</ref><references group="xtra"/>
+
-
[[Category: Bacteria]]
+
[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
[[Category: Max, K E.A.]]
[[Category: Max, K E.A.]]
Line 36: Line 43:
[[Category: Protein binding]]
[[Category: Protein binding]]
[[Category: Secreted]]
[[Category: Secreted]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 3 16:30:24 2009''
 

Revision as of 09:51, 21 May 2014

Structural and energetic determinants for hyperstable variants of GB1 obtained from in-vitro evolution

3fil, resolution 0.88Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fil"
Views
Personal tools
Navigation
Toolbox