1nat
From Proteopedia
(New page: 200px<br /><applet load="1nat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nat, resolution 2.45Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1nat.gif|left|200px]]<br /><applet load="1nat" size=" | + | [[Image:1nat.gif|left|200px]]<br /><applet load="1nat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nat, resolution 2.45Å" /> | caption="1nat, resolution 2.45Å" /> | ||
'''CRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILIS'''<br /> | '''CRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Spo0F is a secondary messenger in the "two-component" system controlling | + | Spo0F is a secondary messenger in the "two-component" system controlling the sporulation of Bacillus subtilis. Spo0F, like the chemotaxis protein CheY, is a single-domain protein homologous to the N-terminal activator domain of the response regulators. We recently reported the crystal structure of a phosphatase-resistant mutant Y13S of Spo0F with Ca2+ bound in the active site. The crystal structure of wild-type Spo0F in the absence of a metal ion is presented here. A comparison of the two structures reveals that the cation induces significant changes in the active site. In the present wild-type structure, the carboxylate of Asp11 points away from the center of the active site, whereas when coordinated to the Ca2+, as in the earlier structure, it points toward the active site. In addition, Asp54, the site of phosphorylation, is blocked by a salt bridge interaction of an Arg side chain from a neighboring molecule. From fluorescence quenching studies with Spo0F Y13W, we found that only the amino acid Arg binds to Spo0F in a saturable manner (Kd = 15 mM). This observation suggests that a small molecule with a shape complementary to the active site and having a guanidinium group might inhibit phosphotransfer between response regulators and their cognate histidine kinases. |
==About this Structure== | ==About this Structure== | ||
| - | 1NAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1NAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hoch, J | + | [[Category: Hoch, J A.]] |
[[Category: Madhusudan]] | [[Category: Madhusudan]] | ||
| - | [[Category: Varughese, K | + | [[Category: Varughese, K I.]] |
| - | [[Category: Whiteley, J | + | [[Category: Whiteley, J M.]] |
| - | [[Category: Xuong, N | + | [[Category: Xuong, N H.]] |
[[Category: Zapf, J.]] | [[Category: Zapf, J.]] | ||
[[Category: aspartate pocket]] | [[Category: aspartate pocket]] | ||
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[[Category: two component system]] | [[Category: two component system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:03 2008'' |
Revision as of 12:04, 21 February 2008
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CRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILIS
Overview
Spo0F is a secondary messenger in the "two-component" system controlling the sporulation of Bacillus subtilis. Spo0F, like the chemotaxis protein CheY, is a single-domain protein homologous to the N-terminal activator domain of the response regulators. We recently reported the crystal structure of a phosphatase-resistant mutant Y13S of Spo0F with Ca2+ bound in the active site. The crystal structure of wild-type Spo0F in the absence of a metal ion is presented here. A comparison of the two structures reveals that the cation induces significant changes in the active site. In the present wild-type structure, the carboxylate of Asp11 points away from the center of the active site, whereas when coordinated to the Ca2+, as in the earlier structure, it points toward the active site. In addition, Asp54, the site of phosphorylation, is blocked by a salt bridge interaction of an Arg side chain from a neighboring molecule. From fluorescence quenching studies with Spo0F Y13W, we found that only the amino acid Arg binds to Spo0F in a saturable manner (Kd = 15 mM). This observation suggests that a small molecule with a shape complementary to the active site and having a guanidinium group might inhibit phosphotransfer between response regulators and their cognate histidine kinases.
About this Structure
1NAT is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis., Madhusudan M, Zapf J, Hoch JA, Whiteley JM, Xuong NH, Varughese KI, Biochemistry. 1997 Oct 21;36(42):12739-45. PMID:9335530
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