We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1m98

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1m98" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m98, resolution 2.10&Aring;" /> '''Crystal Structure of...)
Line 1: Line 1:
-
[[Image:1m98.gif|left|200px]]<br /><applet load="1m98" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1m98.gif|left|200px]]<br /><applet load="1m98" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m98, resolution 2.10&Aring;" />
caption="1m98, resolution 2.10&Aring;" />
'''Crystal Structure of Orange Carotenoid Protein'''<br />
'''Crystal Structure of Orange Carotenoid Protein'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1M98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima] with SUC, CL and HEQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M98 OCA].
+
1M98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=HEQ:'>HEQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M98 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Arthrospira maxima]]
[[Category: Arthrospira maxima]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Kerfeld, C.A.]]
+
[[Category: Kerfeld, C A.]]
[[Category: Krogmann, D.]]
[[Category: Krogmann, D.]]
-
[[Category: Sawaya, M.R.]]
+
[[Category: Sawaya, M R.]]
[[Category: Vishnu, B.]]
[[Category: Vishnu, B.]]
-
[[Category: Yeates, T.O.]]
+
[[Category: Yeates, T O.]]
[[Category: CL]]
[[Category: CL]]
[[Category: HEQ]]
[[Category: HEQ]]
Line 23: Line 23:
[[Category: carotenoid binding protein]]
[[Category: carotenoid binding protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:15:01 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:53 2008''

Revision as of 11:52, 21 February 2008


1m98, resolution 2.10Å

Drag the structure with the mouse to rotate

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 with , and as ligands. 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

Page seeded by OCA on Thu Feb 21 13:52:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools