1nat: Difference between revisions

Revision as of 14:09, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nat.png

Template:STRUCTURE 1nat

CRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILISCRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILIS

Template:ABSTRACT PUBMED 9335530

About this StructureAbout this Structure

1NAT is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 14:09:26 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nat.gif|left|200px]]
+{{Seed}}
+[[Image:1nat.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nat|  PDB=1nat  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF SPOOF FROM BACILLUS SUBTILIS'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9335530}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9335530 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9335530}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Sporulation response regulator]]
 [[Category: Two component system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:18:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:09:26 2008''