1nat

<table><tr><td colspan='2'>[[1nat]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NAT FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPO0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nat OCA], [http://pdbe.org/1nat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nat RCSB], [http://www.ebi.ac.uk/pdbsum/1nat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nat ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SP0F_BACSU SP0F_BACSU]] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9335530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus globigii migula 1900]]

[[Category: Hoch, J A]]

[[Category: Varughese, K I]]

[[Category: Whiteley, J M]]

[[Category: Xuong, N H]]

[[Category: Zapf, J]]

[[Category: Two component system]]