2c7l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c7l.gif|left|200px]]<br /><applet load="2c7l" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2c7l.gif|left|200px]]
-
caption="2c7l, resolution 2.85&Aring;" />
+
 
-
'''LOW TEMPERATURE STRUCTURE OF PHYCOERYTHROCYANIN FROM MASTIGOCLADUS LAMINOSUS'''<br />
+
{{Structure
 +
|PDB= 2c7l |SIZE=350|CAPTION= <scene name='initialview01'>2c7l</scene>, resolution 2.85&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Cyc+Binding+Site+For+Chain+B'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene> and <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''LOW TEMPERATURE STRUCTURE OF PHYCOERYTHROCYANIN FROM MASTIGOCLADUS LAMINOSUS'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2C7L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus] with <scene name='pdbligand=BLA:'>BLA</scene> and <scene name='pdbligand=CYC:'>CYC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cyc+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7L OCA].
+
2C7L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7L OCA].
==Reference==
==Reference==
-
Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin., Schmidt M, Krasselt A, Reuter W, Biochim Biophys Acta. 2006 Jan;1764(1):55-62. Epub 2005 Nov 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16377266 16377266]
+
Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin., Schmidt M, Krasselt A, Reuter W, Biochim Biophys Acta. 2006 Jan;1764(1):55-62. Epub 2005 Nov 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16377266 16377266]
[[Category: Mastigocladus laminosus]]
[[Category: Mastigocladus laminosus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 28: Line 37:
[[Category: phycoviolobilin]]
[[Category: phycoviolobilin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:45 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:56 2008''

Revision as of 14:12, 20 March 2008


PDB ID 2c7l

Drag the structure with the mouse to rotate
, resolution 2.85Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



LOW TEMPERATURE STRUCTURE OF PHYCOERYTHROCYANIN FROM MASTIGOCLADUS LAMINOSUS


Overview

Phycoerythrocyanin is the only cyanobacterial phycobiliprotein containing phycoviolobilin as a chromophore. The phycoviolobilin chromophore is photo-reactive; upon irradiation, the chromophore undergoes a Z/E-isomerization involving the rotation of pyrrole-ring D. We have determined the structure of trimeric phycoerythrocyanin at three different experimental settings: monochromatically at 110 K and 295 K as well as with the Laue method at 288 K. Based on their chemical structures, the restraints for the phycoviolobilin of the alpha-subunit and for the phycocyanobilin chromophores of the beta-subunit were newly generated, which allows a chemically meaningful refinement of both chromophores. All three phycoerythrocyanin structures are very similar; the subunits match within 0.5 A. The detailed comparison of the data obtained with the different measurements provided information about the protein properties around the phycoviolobilin chromophore. For the first time, crystals of a phycobilisome protein are used successfully with the Laue technique. This paves the way for time-resolved macromolecular crystallography, which is able to elucidate the exact mechanisms of the phycoviolobilin photoactivity including the protein involvement.

About this Structure

2C7L is a Protein complex structure of sequences from Mastigocladus laminosus. Full crystallographic information is available from OCA.

Reference

Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin., Schmidt M, Krasselt A, Reuter W, Biochim Biophys Acta. 2006 Jan;1764(1):55-62. Epub 2005 Nov 21. PMID:16377266

Page seeded by OCA on Thu Mar 20 16:11:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools