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	[[Category: Hemmings, A M.]]		[[Category: Hemmings, A M.]]
	[[Category: James, R.]]		[[Category: James, R.]]
-	[[Category: Kleanthous, C.]]
	[[Category: Kuhlmann, U C.]]		[[Category: Kuhlmann, U C.]]
	[[Category: Moore, G R.]]		[[Category: Moore, G R.]]

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Revision as of 19:53, 19 December 2012

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1mnm, resolution 2.25Å ()
Structural annotation: Resources: CATH : 1Mnmc00, 1Mnmd00 InterPro : Ipr002100, Ipr001356, Ipr012287, Ipr009057 Pfam : PF00319, PF00046 SCOP : d1mnma_, d1mnmb_, d1mnmc_, d1mnmd_ UniProt : P11746, Q6B2C0
Functional annotation: Cellular component: nuclear chromatin nucleus Biological process: regulation of transcription from RNA polymerase II promoter cell cycle transcription DNA replication initiation regulation of transcription, DNA-dependent donor selection regulation of transcription Molecular function: DNA bending activity sequence-specific DNA binding transcription factor activity DNA replication origin binding DNA binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

spinqualitylabelsall models YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE (PDB entry 1mnm) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image The structure of a complex containing the homeodomain repressor protein MATalpha2 and the MADS-box transcription factor MCM1 bound to DNA has been determined by X-ray crystallography at 2.25 A resolution. [1]

• Kleanthous C, Kuhlmann UC, Pommer AJ, Ferguson N, Radford SE, Moore GR, James R, Hemmings AM. Structural and mechanistic basis of immunity toward endonuclease colicins. Nat Struct Biol. 1999 Mar;6(3):243-52. PMID:10074943 doi:http://dx.doi.org/10.1038/6683
• Levin KB, Dym O, Albeck S, Magdassi S, Keeble AH, Kleanthous C, Tawfik DS. Following evolutionary paths to protein-protein interactions with high affinity and selectivity. Nat Struct Mol Biol. 2009 Oct;16(10):1049-55. Epub 2009 Sep 13. PMID:19749752 doi:10.1038/nsmb.1670

1. ↑ MCM1 bound to DNA

See Also

• Lipase, the main article in Proteopedia.
• Molecular Playground/Pancreatic Lipase
• Lipase in Wikipedia

Additional Literature

• Marques SM, Esteves da Silva JC. Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. IUBMB Life. 2009 Jan;61(1):6-17. PMID:18949818 doi:10.1002/iub.134
• Inouye S. Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions. Cell Mol Life Sci. 2010 Feb;67(3):387-404. Epub 2009 Oct 27. PMID:19859663 doi:10.1007/s00018-009-0170-8

External Resources

• Yahoo news coverage of luciferase studies funded research for military applications
• Luciferase at Wikipedia
• Luciferase: June 2006 Molecule of the Month as part of the series of tutorials that are at the RCSB Protein Data Bank and written by

Amino Terminus

Carboxy Terminus