3los
From Proteopedia
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[[Image:3los.png|left|200px]] | [[Image:3los.png|left|200px]] | ||
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{{STRUCTURE_3los| PDB=3los | SCENE= }} | {{STRUCTURE_3los| PDB=3los | SCENE= }} | ||
===Atomic Model of Mm-cpn in the Closed State=== | ===Atomic Model of Mm-cpn in the Closed State=== | ||
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{{ABSTRACT_PUBMED_20090755}} | {{ABSTRACT_PUBMED_20090755}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3los]] is a 16 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Methanococcus_maripaludis Methanococcus maripaludis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3iye 3iye]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOS OCA]. | + | [[3los]] is a 16 chain structure of [[Chaperonin]] and [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Methanococcus_maripaludis Methanococcus maripaludis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3iye 3iye]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LOS OCA]. |
==See Also== | ==See Also== | ||
| - | *[[Heat Shock Proteins]] | + | *[[Chaperonin|Chaperonin]] |
| + | *[[Heat Shock Proteins|Heat Shock Proteins]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020090755</ref><references group="xtra"/> |
[[Category: Methanococcus maripaludis]] | [[Category: Methanococcus maripaludis]] | ||
[[Category: Baker, M L.]] | [[Category: Baker, M L.]] | ||
Revision as of 11:06, 27 July 2012
Contents |
Atomic Model of Mm-cpn in the Closed State
Template:ABSTRACT PUBMED 20090755
About this Structure
3los is a 16 chain structure of Chaperonin and Heat Shock Proteins with sequence from Methanococcus maripaludis. This structure supersedes the now removed PDB entry 3iye. Full crystallographic information is available from OCA.
See Also
Reference
- Zhang J, Baker ML, Schroder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W. Mechanism of folding chamber closure in a group II chaperonin. Nature. 2010 Jan 21;463(7279):379-83. PMID:20090755 doi:10.1038/nature08701
Categories: Methanococcus maripaludis | Baker, M L. | Chiu, W. | Dougherty, M. | Douglas, N R. | Frydman, J. | Fu, C J. | Jakana, J. | Levitt, M. | Ludtke, S J. | Reissmann, S. | Schroeder, G. | Zhang, J. | Atp-binding | Chaperone | Group ii chaperonin | Methanococcus maripaludi | Mm-cpn | Nucleotide-binding | Protein folding | Single particle reconstruction
