2a18: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a18 ConSurf].
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Revision as of 19:22, 7 February 2016

carboxysome shell protein ccmK4, crystal form 2carboxysome shell protein ccmK4, crystal form 2

Structural highlights

2a18 is a 3 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:ccmK4 (Aphanocapsa sp. (strain N-1))
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CCMK4_SYNY3] May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial microcompartments are primitive organelles composed entirely of protein subunits. Genomic sequence databases reveal the widespread occurrence of microcompartments across diverse microbes. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. We report three-dimensional crystal structures of multiple carboxysome shell proteins, revealing a hexameric unit as the basic microcompartment building block and showing how these hexamers assemble to form flat facets of the polyhedral shell. The structures suggest how molecular transport across the shell may be controlled and how structural variations might govern the assembly and architecture of these subcellular compartments.

Protein structures forming the shell of primitive bacterial organelles.,Kerfeld CA, Sawaya MR, Tanaka S, Nguyen CV, Phillips M, Beeby M, Yeates TO Science. 2005 Aug 5;309(5736):936-8. PMID:16081736[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Kerfeld CA, Sawaya MR, Tanaka S, Nguyen CV, Phillips M, Beeby M, Yeates TO. Protein structures forming the shell of primitive bacterial organelles. Science. 2005 Aug 5;309(5736):936-8. PMID:16081736 doi:309/5736/936

2a18, resolution 2.28Å

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OCA