View source for 3mp9


==Structure of Streptococcal protein G B1 domain at pH 3.0==
<StructureSection load='3mp9' size='340' side='right'caption='[[3mp9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mp9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsg Strsg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MP9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spg ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1320 STRSG])</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=3mp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mp9 OCA], [https://pdbe.org/3mp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3mp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mp9 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG]] Binds to the constant Fc region of IgG with high affinity. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report chemical shifts for H(N), N, and C' nuclei in the His-tagged B1 domain of protein G (GB1) over a range of pH values from pH 2.0 to 9.0, which fit well to standard pH-dependent equations. We also report a 1.2 A resolution crystal structure of GB1 at pH 3.0. Comparison of this crystal structure with published crystal structures at higher pHs provides details of the structural changes in GB1 associated with protonation of the carboxylate groups, in particular a conformational change in the C-terminus of the protein at low pH. An additional change described recently is not seen in the crystal structure because of crystal contacts. We show that the pH-dependent changes in chemical shifts can be almost entirely understood based on structural changes, thereby providing insight into the relationship between structure and chemical shift. In particular, we describe through-bond effects extending up to five bonds, affecting N and C' but not H(N); through-space effects of carboxylates, which fit well to a simple electric field model; and effects due to conformational change, which have a similar magnitude to many of the direct effects. Finally, we discuss cooperative effects, demonstrating a lack of cooperative unfolding in the helix, and the existence of a beta-sheet "iceberg" extending over three of the four strands. This study therefore extends the application of chemical shifts to understanding protein structure.

Structural origins of pH-dependent chemical shifts in the B1 domain of protein G.,Tomlinson JH, Green VL, Baker PJ, Williamson MP Proteins. 2010 Nov 1;78(14):3000-16. PMID:20715051<ref>PMID:20715051</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mp9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Protein G|Protein G]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Strsg]]
[[Category: Baker, P J]]
[[Category: Green, V L]]
[[Category: Tomlinson, J H]]
[[Category: Williamson, M P]]
[[Category: Igg-binding protein]]
[[Category: Protein binding]]
[[Category: Protein g]]