1lr5
From Proteopedia
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|PDB= 1lr5 |SIZE=350|CAPTION= <scene name='initialview01'>1lr5</scene>, resolution 1.9Å | |PDB= 1lr5 |SIZE=350|CAPTION= <scene name='initialview01'>1lr5</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lrh|1LRH]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr5 OCA], [http://www.ebi.ac.uk/pdbsum/1lr5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lr5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Venis, M.]] | [[Category: Venis, M.]] | ||
[[Category: Woo, E J.]] | [[Category: Woo, E J.]] | ||
| - | [[Category: ZN]] | ||
[[Category: beta jellyroll]] | [[Category: beta jellyroll]] | ||
[[Category: double stranded beta helix]] | [[Category: double stranded beta helix]] | ||
[[Category: germin-like protein]] | [[Category: germin-like protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:18 2008'' |
Revision as of 19:06, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1LRH
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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