1lr5
From Proteopedia
(New page: 200px<br /><applet load="1lr5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lr5, resolution 1.9Å" /> '''Crystal structure of ...) |
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| - | [[Image:1lr5.gif|left|200px]]<br /><applet load="1lr5" size=" | + | [[Image:1lr5.gif|left|200px]]<br /><applet load="1lr5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lr5, resolution 1.9Å" /> | caption="1lr5, resolution 1.9Å" /> | ||
'''Crystal structure of auxin binding protein'''<br /> | '''Crystal structure of auxin binding protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of auxin-binding protein 1 (ABP1) from maize has been | + | The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction. |
==About this Structure== | ==About this Structure== | ||
| - | 1LR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Zea mays]] | [[Category: Zea mays]] | ||
[[Category: Bauley, J.]] | [[Category: Bauley, J.]] | ||
| - | [[Category: Chen, J | + | [[Category: Chen, J G.]] |
[[Category: Marshall, J.]] | [[Category: Marshall, J.]] | ||
| - | [[Category: Napier, R | + | [[Category: Napier, R M.]] |
| - | [[Category: Pickersgill, R | + | [[Category: Pickersgill, R W.]] |
[[Category: Venis, M.]] | [[Category: Venis, M.]] | ||
| - | [[Category: Woo, E | + | [[Category: Woo, E J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: beta jellyroll]] | [[Category: beta jellyroll]] | ||
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[[Category: germin-like protein]] | [[Category: germin-like protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:39 2008'' |
Revision as of 11:47, 21 February 2008
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Crystal structure of auxin binding protein
Overview
The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.
About this Structure
1LR5 is a Single protein structure of sequence from Zea mays with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of auxin-binding protein 1 in complex with auxin., Woo EJ, Marshall J, Bauly J, Chen JG, Venis M, Napier RM, Pickersgill RW, EMBO J. 2002 Jun 17;21(12):2877-85. PMID:12065401
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