1nz0: Difference between revisions
New page: left|200px<br /><applet load="1nz0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nz0, resolution 1.20Å" /> '''RNASE P PROTEIN FROM... |
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[[Image:1nz0.gif|left|200px]]<br /><applet load="1nz0" size=" | [[Image:1nz0.gif|left|200px]]<br /><applet load="1nz0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nz0, resolution 1.20Å" /> | caption="1nz0, resolution 1.20Å" /> | ||
'''RNASE P PROTEIN FROM THERMOTOGA MARITIMA'''<br /> | '''RNASE P PROTEIN FROM THERMOTOGA MARITIMA'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of RNase P protein from the hyperthermophilic bacterium | The structure of RNase P protein from the hyperthermophilic bacterium Thermotoga maritima was determined at 1.2-A resolution by using x-ray crystallography. This protein structure is from an ancestral-type RNase P and bears remarkable similarity to the recently determined structures of RNase P proteins from bacteria that have the distinct, Bacillus type of RNase P. These two types of protein span the extent of bacterial RNase P diversity, so the results generalize the structure of the bacterial RNase P protein. The broad phylogenetic conservation of structure and distribution of potential RNA-binding elements in the RNase P proteins indicate that all of these homologous proteins bind to their cognate RNAs primarily by interaction with the phylogenetically conserved core of the RNA. The protein is found to dimerize through an extensive, well-ordered interface. This dimerization may reflect a mechanism of thermal stability of the protein before assembly with the RNA moiety of the holoenzyme. | ||
==About this Structure== | ==About this Structure== | ||
1NZ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] Full crystallographic information is available from [http:// | 1NZ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZ0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Adams, P | [[Category: Adams, P D.]] | ||
[[Category: BSGC, Berkeley | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
[[Category: Carter, R | [[Category: Carter, R J.]] | ||
[[Category: Harrington, D | [[Category: Harrington, D J.]] | ||
[[Category: Holbrook, S | [[Category: Holbrook, S R.]] | ||
[[Category: Kazantsev, A | [[Category: Kazantsev, A V.]] | ||
[[Category: Krivenko, A | [[Category: Krivenko, A A.]] | ||
[[Category: Pace, N | [[Category: Pace, N R.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alfa-beta sandwich]] | [[Category: alfa-beta sandwich]] | ||
| Line 33: | Line 33: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:36 2008'' | ||
Revision as of 15:11, 21 February 2008
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RNASE P PROTEIN FROM THERMOTOGA MARITIMA
OverviewOverview
The structure of RNase P protein from the hyperthermophilic bacterium Thermotoga maritima was determined at 1.2-A resolution by using x-ray crystallography. This protein structure is from an ancestral-type RNase P and bears remarkable similarity to the recently determined structures of RNase P proteins from bacteria that have the distinct, Bacillus type of RNase P. These two types of protein span the extent of bacterial RNase P diversity, so the results generalize the structure of the bacterial RNase P protein. The broad phylogenetic conservation of structure and distribution of potential RNA-binding elements in the RNase P proteins indicate that all of these homologous proteins bind to their cognate RNAs primarily by interaction with the phylogenetically conserved core of the RNA. The protein is found to dimerize through an extensive, well-ordered interface. This dimerization may reflect a mechanism of thermal stability of the protein before assembly with the RNA moiety of the holoenzyme.
About this StructureAbout this Structure
1NZ0 is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as Ribonuclease P, with EC number 3.1.26.5 Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structure of RNase P protein from Thermotoga maritima., Kazantsev AV, Krivenko AA, Harrington DJ, Carter RJ, Holbrook SR, Adams PD, Pace NR, Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7497-502. Epub 2003 Jun 10. PMID:12799461
Page seeded by OCA on Thu Feb 21 14:11:36 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Ribonuclease P
- Single protein
- Thermotoga maritima
- Adams, P D.
- BSGC, Berkeley Structural Genomics Center.
- Carter, R J.
- Harrington, D J.
- Holbrook, S R.
- Kazantsev, A V.
- Krivenko, A A.
- Pace, N R.
- SO4
- Alfa-beta sandwich
- Berkeley structural genomics center
- Bsgc structure funded by nih
- Dimer
- Endonuclease
- Protein structure initiative
- Psi
- Rnase
- Structural genomics