1pc3: Difference between revisions

Revision as of 15:27, 21 February 2008

Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis.

OverviewOverview

The 2.16 A structure of the phosphate-bound PstS-1, the primary extracellular receptor for the ABC phosphate transporter and immunodominant species-specific antigen of Mycobacterium tuberculosis, has been determined. The phosphate, completely engulfed in the cleft between two domains, is bound by 13 hydrogen bonds, 11 of which are formed with NH and OH dipolar donor groups. The further presence of two acidic residues, which serve as acceptors of the protonated phosphate, is key to conferring stringent specificity. The ion-dipole interactions between the phosphate and dipolar groups compensate the ligand's isolated negative charges. Moreover, the surprise finding that the electrostatic surface in and around the cleft is intensely negative demonstrates the power of ion-dipole interactions in anion binding and electrostatic balance. Additional functional features include both the flexible N-terminal segment that tethers PstS-1 on the cell surface and the hinge between the two domains, which should facilitate snaring the phosphate in the medium.

About this StructureAbout this Structure

1PC3 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions., Vyas NK, Vyas MN, Quiocho FA, Structure. 2003 Jul;11(7):765-74. PMID:12842040

Page seeded by OCA on Thu Feb 21 14:27:17 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1pc3.gif|left|200px]]<br /><applet load="1pc3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pc3.gif|left|200px]]<br /><applet load="1pc3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pc3, resolution 2.16&Aring;" />
 '''Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis.'''<br />
 ==Overview==
-The 2.16 A structure of the phosphate-bound PstS-1, the primary, extracellular receptor for the ABC phosphate transporter and, immunodominant species-specific antigen of Mycobacterium tuberculosis, has, been determined. The phosphate, completely engulfed in the cleft between, two domains, is bound by 13 hydrogen bonds, 11 of which are formed with NH, and OH dipolar donor groups. The further presence of two acidic residues, which serve as acceptors of the protonated phosphate, is key to conferring, stringent specificity. The ion-dipole interactions between the phosphate, and dipolar groups compensate the ligand's isolated negative charges., Moreover, the surprise finding that the electrostatic surface in and, around the cleft is intensely negative demonstrates the power of, ion-dipole interactions in anion binding and electrostatic balance., Additional functional features include both the flexible N-terminal, segment that tethers PstS-1 on the cell surface and the hinge between the, two domains, which should facilitate snaring the phosphate in the medium.
+The 2.16 A structure of the phosphate-bound PstS-1, the primary extracellular receptor for the ABC phosphate transporter and immunodominant species-specific antigen of Mycobacterium tuberculosis, has been determined. The phosphate, completely engulfed in the cleft between two domains, is bound by 13 hydrogen bonds, 11 of which are formed with NH and OH dipolar donor groups. The further presence of two acidic residues, which serve as acceptors of the protonated phosphate, is key to conferring stringent specificity. The ion-dipole interactions between the phosphate and dipolar groups compensate the ligand's isolated negative charges. Moreover, the surprise finding that the electrostatic surface in and around the cleft is intensely negative demonstrates the power of ion-dipole interactions in anion binding and electrostatic balance. Additional functional features include both the flexible N-terminal segment that tethers PstS-1 on the cell surface and the hinge between the two domains, which should facilitate snaring the phosphate in the medium.
 ==About this Structure==
-PC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PC3 OCA].
+PC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC3 OCA].
 ==Reference==
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 [[Category: Mycobacterium tuberculosis]]
 [[Category: Single protein]]
-[[Category: Quiocho, F.A.]]
+[[Category: Quiocho, F A.]]
-[[Category: Vyas, M.N.]]
+[[Category: Vyas, M N.]]
-[[Category: Vyas, N.K.]]
+[[Category: Vyas, N K.]]
 [[Category: PO4]]
 [[Category: crystal structure]]
@@ Line 24: / Line 24: @@
 [[Category: phosphate transport receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:40:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:17 2008''