1pc3: Difference between revisions
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[[Image:1pc3.gif|left|200px]] | [[Image:1pc3.gif|left|200px]] | ||
'''Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis.''' | {{Structure | ||
|PDB= 1pc3 |SIZE=350|CAPTION= <scene name='initialview01'>1pc3</scene>, resolution 2.16Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= | |||
|GENE= PSTS1 OR PHOS1 OR RV0934 OR MT0961 OR MTCY08D9.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |||
}} | |||
'''Crystal structure of the extracellular phosphate ABC transport receptor (PstS-1) and immunodominant antigen of M. tuberculosis.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PC3 is a [ | 1PC3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC3 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12842040 12842040] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: | [[Category: electrostatic]] | ||
[[Category: immonodominant antigen]] | [[Category: immonodominant antigen]] | ||
[[Category: ion-dipole | [[Category: ion-dipole interaction]] | ||
[[Category: mycobacterium tuberculosis]] | [[Category: mycobacterium tuberculosis]] | ||
[[Category: phosphate transport receptor]] | [[Category: phosphate transport receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:30 2008'' | ||
Revision as of 14:22, 20 March 2008
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| , resolution 2.16Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PSTS1 OR PHOS1 OR RV0934 OR MT0961 OR MTCY08D9.05C (Mycobacterium tuberculosis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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