1pey

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(New page: 200px<br /><applet load="1pey" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pey, resolution 2.25&Aring;" /> '''Crystal structure of...)
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[[Image:1pey.gif|left|200px]]<br /><applet load="1pey" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pey.gif|left|200px]]<br /><applet load="1pey" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pey, resolution 2.25&Aring;" />
caption="1pey, resolution 2.25&Aring;" />
'''Crystal structure of the Response Regulator Spo0F complexed with Mn2+'''<br />
'''Crystal structure of the Response Regulator Spo0F complexed with Mn2+'''<br />
==Overview==
==Overview==
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As a part of studies on the structural characterization of the components, of the sporulation phosphorelay in Bacillus subtilis, the crystal, structure of the manganese derivative of an intermediate signal, transducer, Spo0F, has been elucidated at 2.25 A resolution. The calcium, complex and the apo structures have been analyzed previously. In apo, Spo0F, the active-site cation cavity is only partially formed and it only, becomes completed upon metal coordination. The carbonyl of Lys56 is, coordinated to the metal and interestingly the side chain of Lys56 exists, in a variety of conformations in the three crystal structures of Spo0F., The affinity of the magnesium ion for Spo0F is in fact low; however, it, binds Spo0F when it is in complex with Spo0B. It is proposed that the, existence of a deep pocket which extends from the surface to the metal, site could attract and direct the metal, thereby facilitating the metal, binding of the complex.
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As a part of studies on the structural characterization of the components of the sporulation phosphorelay in Bacillus subtilis, the crystal structure of the manganese derivative of an intermediate signal transducer, Spo0F, has been elucidated at 2.25 A resolution. The calcium complex and the apo structures have been analyzed previously. In apo Spo0F, the active-site cation cavity is only partially formed and it only becomes completed upon metal coordination. The carbonyl of Lys56 is coordinated to the metal and interestingly the side chain of Lys56 exists in a variety of conformations in the three crystal structures of Spo0F. The affinity of the magnesium ion for Spo0F is in fact low; however, it binds Spo0F when it is in complex with Spo0B. It is proposed that the existence of a deep pocket which extends from the surface to the metal site could attract and direct the metal, thereby facilitating the metal binding of the complex.
==About this Structure==
==About this Structure==
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1PEY 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PEY OCA].
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1PEY 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEY OCA].
==Reference==
==Reference==
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[[Category: Mukhopadhyay, D.]]
[[Category: Mukhopadhyay, D.]]
[[Category: Sen, U.]]
[[Category: Sen, U.]]
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[[Category: Varughese, K.I.]]
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[[Category: Varughese, K I.]]
[[Category: Zapf, J.]]
[[Category: Zapf, J.]]
[[Category: MN]]
[[Category: MN]]
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[[Category: cation binding]]
[[Category: cation binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:45:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:09 2008''

Revision as of 12:28, 21 February 2008


1pey, resolution 2.25Å

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Crystal structure of the Response Regulator Spo0F complexed with Mn2+

Overview

As a part of studies on the structural characterization of the components of the sporulation phosphorelay in Bacillus subtilis, the crystal structure of the manganese derivative of an intermediate signal transducer, Spo0F, has been elucidated at 2.25 A resolution. The calcium complex and the apo structures have been analyzed previously. In apo Spo0F, the active-site cation cavity is only partially formed and it only becomes completed upon metal coordination. The carbonyl of Lys56 is coordinated to the metal and interestingly the side chain of Lys56 exists in a variety of conformations in the three crystal structures of Spo0F. The affinity of the magnesium ion for Spo0F is in fact low; however, it binds Spo0F when it is in complex with Spo0B. It is proposed that the existence of a deep pocket which extends from the surface to the metal site could attract and direct the metal, thereby facilitating the metal binding of the complex.

About this Structure

1PEY is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.

Reference

Metals in the sporulation phosphorelay: manganese binding by the response regulator Spo0F., Mukhopadhyay D, Sen U, Zapf J, Varughese KI, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):638-45. Epub 2004, Mar 23. PMID:15039551

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