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1lrh

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(New page: 200px<br /><applet load="1lrh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lrh, resolution 1.9&Aring;" /> '''Crystal structure of ...)
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[[Image:1lrh.gif|left|200px]]<br /><applet load="1lrh" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lrh.gif|left|200px]]<br /><applet load="1lrh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lrh, resolution 1.9&Aring;" />
caption="1lrh, resolution 1.9&Aring;" />
'''Crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid'''<br />
'''Crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid'''<br />
==Overview==
==Overview==
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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.
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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==
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1LRH 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 and NLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LRH OCA].
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1LRH 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> and <scene name='pdbligand=NLA:'>NLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LRH OCA].
==Reference==
==Reference==
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[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Bauly, J.]]
[[Category: Bauly, J.]]
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[[Category: Chen, J.G.]]
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[[Category: Chen, J G.]]
[[Category: Marshall, J.]]
[[Category: Marshall, J.]]
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[[Category: Napier, R.M.]]
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[[Category: Napier, R M.]]
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[[Category: Pickersgill, R.W.]]
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[[Category: Pickersgill, R W.]]
[[Category: Venis, M.]]
[[Category: Venis, M.]]
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[[Category: Woo, E.J.]]
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[[Category: Woo, E J.]]
[[Category: NLA]]
[[Category: NLA]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: germin like protein]]
[[Category: germin like protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:48:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:40 2008''

Revision as of 11:47, 21 February 2008

Image:1lrh.gif

1lrh, resolution 1.9Å

Drag the structure with the mouse to rotate

Crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid

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

1LRH is a Single protein structure of sequence from Zea mays with and as ligands. 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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