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1toa

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(New page: 200px<br /><applet load="1toa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1toa, resolution 1.8&Aring;" /> '''PERIPLASMIC ZINC BIND...)
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[[Image:1toa.gif|left|200px]]<br /><applet load="1toa" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1toa.gif|left|200px]]<br /><applet load="1toa" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1toa, resolution 1.8&Aring;" />
caption="1toa, resolution 1.8&Aring;" />
'''PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM'''<br />
'''PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM'''<br />
==Overview==
==Overview==
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The crystal structure of recombinant TroA, a zinc-binding protein, component of an ATP-binding cassette transport system in Treponema, pallidum, was determined at a resolution of 1.8 A. The organization of the, protein is largely similar to other periplasmic ligand-binding proteins, (PLBP), in that two independent globular domains interact with each other, to create a zinc-binding cleft between them. The structure has one bound, zinc pentavalently coordinated to residues from both domains. Unlike, previous PLBP structures that have an interdomain hinge composed of, beta-strands, the N- and C-domains of TroA are linked by a single long, backbone helix. This unique backbone helical conformation was possibly, adopted to limit the hinge motion associated with ligand exchange.
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The crystal structure of recombinant TroA, a zinc-binding protein component of an ATP-binding cassette transport system in Treponema pallidum, was determined at a resolution of 1.8 A. The organization of the protein is largely similar to other periplasmic ligand-binding proteins (PLBP), in that two independent globular domains interact with each other to create a zinc-binding cleft between them. The structure has one bound zinc pentavalently coordinated to residues from both domains. Unlike previous PLBP structures that have an interdomain hinge composed of beta-strands, the N- and C-domains of TroA are linked by a single long backbone helix. This unique backbone helical conformation was possibly adopted to limit the hinge motion associated with ligand exchange.
==About this Structure==
==About this Structure==
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1TOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TOA OCA].
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1TOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TOA OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Treponema pallidum]]
[[Category: Treponema pallidum]]
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[[Category: Deka, R.K.]]
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[[Category: Deka, R K.]]
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[[Category: Hasemann, C.A.]]
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[[Category: Hasemann, C A.]]
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[[Category: Lee, Y.H.]]
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[[Category: Lee, Y H.]]
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[[Category: Norgard, M.V.]]
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[[Category: Norgard, M V.]]
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[[Category: Radolf, J.D.]]
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[[Category: Radolf, J D.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc binding protein]]
[[Category: zinc binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:27:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:39 2008''

Revision as of 13:15, 21 February 2008


1toa, resolution 1.8Å

Drag the structure with the mouse to rotate

PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM

Overview

The crystal structure of recombinant TroA, a zinc-binding protein component of an ATP-binding cassette transport system in Treponema pallidum, was determined at a resolution of 1.8 A. The organization of the protein is largely similar to other periplasmic ligand-binding proteins (PLBP), in that two independent globular domains interact with each other to create a zinc-binding cleft between them. The structure has one bound zinc pentavalently coordinated to residues from both domains. Unlike previous PLBP structures that have an interdomain hinge composed of beta-strands, the N- and C-domains of TroA are linked by a single long backbone helix. This unique backbone helical conformation was possibly adopted to limit the hinge motion associated with ligand exchange.

About this Structure

1TOA is a Single protein structure of sequence from Treponema pallidum with and as ligands. Full crystallographic information is available from OCA.

Reference

Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone., Lee YH, Deka RK, Norgard MV, Radolf JD, Hasemann CA, Nat Struct Biol. 1999 Jul;6(7):628-33. PMID:10404217

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