This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kby

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kby.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kby.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kby| PDB=1kby | SCENE= }}
{{STRUCTURE_1kby| PDB=1kby | SCENE= }}
-
'''Structure of Photosynthetic Reaction Center with bacteriochlorophyll-bacteriopheophytin heterodimer'''
+
===Structure of Photosynthetic Reaction Center with bacteriochlorophyll-bacteriopheophytin heterodimer===
-
==Overview==
+
<!--
-
Crystals have been obtained of reaction centers of the heterodimer mutant that has significantly different properties than wild type due to the primary donor being formed from both a bacteriochlorophyll and bacteriopheophytin rather than two bacteriochlorophylls as found for wild type. The crystals belong to the trigonal space group P3(1)21 and the structure has been refined to a resolution limit of 2.55 A with an R factor of 19.0%. The electron density maps confirm that a primary donor does indeed contain a bacteriopheophytin due to the His to Leu substitution at M202 that coordinates the corresponding bacteriochlorophyll in wild-type. Other structural changes compared to wild type are relatively minor with the relative orientation and positioning of the two tetrapyrroles forming the primary donor being unchanged within the error. Compared to wild type, the only significant alterations are small shifts of residues M196 to M206, a rotation of the side chain of Ile M206, and the loss of a bound water molecule that in wild-type is hydrogen-bonded to both His M202 and the bacteriochlorophyll monomer on the active branch. Since hydrogen-bonding interactions strongly influence the energies of tetrapyrroles, the loss of the water molecule should result in changes in the energies of the bacteriochlorophyll monomer that contributes to the observed functional differences with wild-type.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16228547}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16228547 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16228547}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Magee, C.]]
[[Category: Magee, C.]]
[[Category: Transmembrane alpha helix]]
[[Category: Transmembrane alpha helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:33:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:06:24 2008''

Revision as of 07:06, 2 July 2008

Image:1kby.png

Template:STRUCTURE 1kby

Structure of Photosynthetic Reaction Center with bacteriochlorophyll-bacteriopheophytin heterodimer

Template:ABSTRACT PUBMED 16228547

About this Structure

1KBY is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

The structure of the heterodimer reaction center from Rhodobacter sphaeroides at 2.55 a resolution., Camara-Artigas A, Magee C, Goetsch A, Allen JP, Photosynth Res. 2002;74(1):87-93. PMID:16228547

Page seeded by OCA on Wed Jul 2 10:06:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kby"
Personal tools