1gjt: Difference between revisions

Revision as of 13:50, 21 February 2008

SOLUTION STRUCTURE OF THE ALBUMIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G

OverviewOverview

We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.

About this StructureAbout this Structure

1GJT is a Single protein structure of sequence from Streptococcus sp. group g. Full crystallographic information is available from OCA.

ReferenceReference

Structure, specificity, and mode of interaction for bacterial albumin-binding modules., Johansson MU, Frick IM, Nilsson H, Kraulis PJ, Hober S, Jonasson P, Linhult M, Nygren PA, Uhlen M, Bjorck L, Drakenberg T, Forsen S, Wikstrom M, J Biol Chem. 2002 Mar 8;277(10):8114-20. Epub 2001 Dec 18. PMID:11751858

Page seeded by OCA on Thu Feb 21 12:50:54 2008

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OCA

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-[[Image:1gjt.gif|left|200px]]<br /><applet load="1gjt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gjt.gif|left|200px]]<br /><applet load="1gjt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gjt" />
 '''SOLUTION STRUCTURE OF THE ALBUMIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G'''<br />
 ==Overview==
-We have determined the solution structure of an albumin binding domain of, protein G, a surface protein of group C and G streptococci. We find that, it folds into a left handed three-helix bundle similar to the albumin, binding domain of protein PAB from Peptostreptococcus magnus. The two, domains share 59% sequence identity, are thermally very stable, and bind, to the same site on human serum albumin. The albumin binding site, the, first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third, helix and includes the most conserved region of GA modules. The two GA, modules have different affinities for albumin from different species, and, their albumin binding patterns correspond directly to the host specificity, of C/G streptococci and P. magnus, respectively. These studies of the, evolution, structure, and binding properties of the GA module emphasize, the power of bacterial adaptation and underline ecological and medical, problems connected with the use of antibiotics.
+We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.
 ==About this Structure==
-GJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp._group_g Streptococcus sp. group g]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GJT OCA].
+GJT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1GJT OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Bjorck, L.]]
 [[Category: Drakenbergforsen, S.]]
-[[Category: Frick, I.M.]]
+[[Category: Frick, I M.]]
 [[Category: Hober, S.]]
-[[Category: Johansson, M.U.]]
+[[Category: Johansson, M U.]]
 [[Category: Jonasson, P.]]
-[[Category: Kraulis, P.J.]]
+[[Category: Kraulis, P J.]]
 [[Category: Nilsson, H.]]
-[[Category: Nygren, P.A.]]
+[[Category: Nygren, P A.]]
 [[Category: Uhlen, M.]]
 [[Category: Wikstrom, M.]]
@@ Line 28: / Line 28: @@
 [[Category: protein g]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:06:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:54 2008''