1zax: Difference between revisions
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[[Image:1zax. | {{Seed}} | ||
[[Image:1zax.png|left|200px]] | |||
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{{STRUCTURE_1zax| PDB=1zax | SCENE= }} | {{STRUCTURE_1zax| PDB=1zax | SCENE= }} | ||
===Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B=== | |||
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(as it appears on PubMed at http://www.pubmed.gov), where 15989950 is the PubMed ID number. | |||
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{{ABSTRACT_PUBMED_15989950}} | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: Translation factor recruitment]] | [[Category: Translation factor recruitment]] | ||
[[Category: X-ray crystallography]] | [[Category: X-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:54:32 2008'' |
Revision as of 05:54, 28 July 2008
Ribosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form BRibosomal Protein L10-L12(NTD) Complex, Space Group P212121, Form B
Template:ABSTRACT PUBMED 15989950
About this StructureAbout this Structure
1ZAX is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation., Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC, Cell. 2005 Jul 1;121(7):991-1004. PMID:15989950
Page seeded by OCA on Mon Jul 28 05:54:32 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Pages with broken file links
- Protein complex
- Thermotoga maritima
- Diaconu, M.
- Fischer, N.
- Harms, J M.
- Kothe, U.
- Rodnina, M V.
- Schluenzen, F.
- Stark, H.
- Tonevitski, A G.
- Wahl, M C.
- Cryo-electron microscopy
- Gtpase stimulation
- L10-l12 complex structure
- L10e structure
- L7/12 ribosomal stalk
- Mechanism of translation
- Rapid kinetic
- Ribosome structure and function
- Thiostrepton loop of 23s rrna
- Translation factor recruitment
- X-ray crystallography