2nzo: Difference between revisions

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[[Image:2nzo.gif|left|200px]]<br /><applet load="2nzo" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2nzo.gif|left|200px]]<br /><applet load="2nzo" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2nzo, resolution 2.000Å" />

'''Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group P 32 2 1'''<br />

==Overview==

Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a, protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive, eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups, (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal, structure of CsaA from the Gram-negative eubacterium Thermus thermophilus, (TtCsaA) and provide a direct structural basis for the interpretation of, previously available biochemical data on BsCsaA. The sequence and, structure of the proposed substrate-binding pocket are analyzed and, discussed. A comparison with the TtCsaA structure reveals a different, pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and, discussed.

Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal structure of CsaA from the Gram-negative eubacterium Thermus thermophilus (TtCsaA) and provide a direct structural basis for the interpretation of previously available biochemical data on BsCsaA. The sequence and structure of the proposed substrate-binding pocket are analyzed and discussed. A comparison with the TtCsaA structure reveals a different pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and discussed.

==About this Structure==

2NZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2NZO OCA].

2NZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZO OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Paetzel, M.]]

[[Category: Shapova, Y.A.]]

[[Category: Shapova, Y A.]]

[[Category: GOL]]

[[Category: beta barrel]]

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[[Category: oligonucleotide/oligosaccharide binding fold]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2nzo.gif|left|200px]]<br /><applet load="2nzo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nzo.gif|left|200px]]<br /><applet load="2nzo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2nzo, resolution 2.000&Aring;" />
 '''Crystal structure of a secretion chaperone CsaA from Bacillus subtilis in the space group P 32 2 1'''<br />
 ==Overview==
-Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a, protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive, eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups, (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal, structure of CsaA from the Gram-negative eubacterium Thermus thermophilus, (TtCsaA) and provide a direct structural basis for the interpretation of, previously available biochemical data on BsCsaA. The sequence and, structure of the proposed substrate-binding pocket are analyzed and, discussed. A comparison with the TtCsaA structure reveals a different, pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and, discussed.
+Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1.9 and 2.0 A, respectively. These structures complement the previously available crystal structure of CsaA from the Gram-negative eubacterium Thermus thermophilus (TtCsaA) and provide a direct structural basis for the interpretation of previously available biochemical data on BsCsaA. The sequence and structure of the proposed substrate-binding pocket are analyzed and discussed. A comparison with the TtCsaA structure reveals a different pattern of electrostatic potential in the vicinity of the binding site, which overlaps with a region of high sequence variability. In addition, the dimerization interface of this homodimeric protein is analyzed and discussed.
 ==About this Structure==
-NZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NZO OCA].
+NZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZO OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Paetzel, M.]]
-[[Category: Shapova, Y.A.]]
+[[Category: Shapova, Y A.]]
 [[Category: GOL]]
 [[Category: beta barrel]]
@@ Line 21: / Line 21: @@
 [[Category: oligonucleotide/oligosaccharide binding fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:00:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:51 2008''