1hqm: Difference between revisions

New page: left|200px<br /><applet load="1hqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqm, resolution 3.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1hqm.jpg|left|200px]]<br /><applet load="1hqm" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hqm.jpg|left|200px]]<br /><applet load="1hqm" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hqm, resolution 3.3&Aring;" />
caption="1hqm, resolution 3.3&Aring;" />
'''CRYSTAL STRUCTURE OF THERMUS AQUATICUS CORE RNA POLYMERASE-INCLUDES COMPLETE STRUCTURE WITH SIDE-CHAINS (EXCEPT FOR DISORDERED REGIONS)-FURTHER REFINED FROM ORIGINAL DEPOSITION-CONTAINS ADDITIONAL SEQUENCE INFORMATION'''<br />
'''CRYSTAL STRUCTURE OF THERMUS AQUATICUS CORE RNA POLYMERASE-INCLUDES COMPLETE STRUCTURE WITH SIDE-CHAINS (EXCEPT FOR DISORDERED REGIONS)-FURTHER REFINED FROM ORIGINAL DEPOSITION-CONTAINS ADDITIONAL SEQUENCE INFORMATION'''<br />


==Overview==
==Overview==
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition, beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We, show that omega is homologous in sequence and structure to RPB6, an, essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia, coli, overproduction of omega suppresses the assembly defect caused by, substitution of residue 1362 of the largest subunit of RNAP, beta'. In, yeast, overproduction of RPB6 suppresses the assembly defect caused by the, equivalent substitution in the largest subunit of RNAP II, RPB1., High-resolution structural analysis of the omega-beta' interface in, bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP, II, confirms the structural relationship and suggests a "latching", mechanism for the role of omega and RPB6 in promoting RNAP assembly.
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.


==About this Structure==
==About this Structure==
1HQM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1DDQ. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQM OCA].  
1HQM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1DDQ. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQM OCA].  


==Reference==
==Reference==
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[[Category: Bhagat, S.]]
[[Category: Bhagat, S.]]
[[Category: Brunning, A.]]
[[Category: Brunning, A.]]
[[Category: Campbell, E.A.]]
[[Category: Campbell, E A.]]
[[Category: Darst, S.A.]]
[[Category: Darst, S A.]]
[[Category: Ebright, R.H.]]
[[Category: Ebright, R H.]]
[[Category: Minakhin, L.]]
[[Category: Minakhin, L.]]
[[Category: Severinov, K.]]
[[Category: Severinov, K.]]
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[[Category: transferase]]
[[Category: transferase]]


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