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1m98

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|PDB= 1m98 |SIZE=350|CAPTION= <scene name='initialview01'>1m98</scene>, resolution 2.10&Aring;
|PDB= 1m98 |SIZE=350|CAPTION= <scene name='initialview01'>1m98</scene>, resolution 2.10&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=HEQ:3-[18-(4-HYDROXY-2,6,6-TRIMETHYL-CYCLOHEX-1-ENYL)-3,7,12,16-TETRAMETHYL-OCTADECA-1,3,5,7,9,11,13,15, 17-NONAENYL]-2,4,4-TRIMETHYL-CYCLOHEX-2-ENONE'>HEQ</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEQ:3-[18-(4-HYDROXY-2,6,6-TRIMETHYL-CYCLOHEX-1-ENYL)-3,7,12,16-TETRAMETHYL-OCTADECA-1,3,5,7,9,11,13,15,+17-NONAENYL]-2,4,4-TRIMETHYL-CYCLOHEX-2-ENONE'>HEQ</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m98 OCA], [http://www.ebi.ac.uk/pdbsum/1m98 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m98 RCSB]</span>
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}}
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[[Category: Vishnu, B.]]
[[Category: Vishnu, B.]]
[[Category: Yeates, T O.]]
[[Category: Yeates, T O.]]
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[[Category: CL]]
 
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[[Category: HEQ]]
 
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[[Category: SUC]]
 
[[Category: carotenoid binding protein]]
[[Category: carotenoid binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:00 2008''

Revision as of 19:13, 30 March 2008

Image:1m98.gif


PDB ID 1m98

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Orange Carotenoid Protein


Overview

Carotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to light harvesting, they perform an essential role in protecting against light-induced damage by quenching singlet oxygen, superoxide anion radicals, or triplet-state chlorophyll. We have determined the crystal structure of a water-soluble orange carotenoid protein (OCP) isolated from the cyanobacterium Arthrospira maxima at a resolution of 2.1 A. OCP forms a homodimer with one carotenoid molecule per monomer. The carotenoid binding site is lined by a striking number of methionine residues. The structure reveals several possible ways in which the protein environment influences the spectral properties of the pigment and provides insight into how the OCP carries out its putative functions in photoprotection.

About this Structure

1M98 is a Single protein structure of sequence from Arthrospira maxima. Full crystallographic information is available from OCA.

Reference

The crystal structure of a cyanobacterial water-soluble carotenoid binding protein., Kerfeld CA, Sawaya MR, Brahmandam V, Cascio D, Ho KK, Trevithick-Sutton CC, Krogmann DW, Yeates TO, Structure. 2003 Jan;11(1):55-65. PMID:12517340

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