2fgy: Difference between revisions

Revision as of 18:21, 21 February 2008

Beta Carbonic Anhydrase from the Carboxysomal Shell of Halothiobacillus neapolitanus (CsoSCA)

OverviewOverview

CsoSCA (formerly CsoS3) is a bacterial carbonic anhydrase localized in the shell of a cellular microcompartment called the carboxysome, where it converts HCO(3)(-) to CO(2) for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase (RuBisCO). CsoSCA lacks significant sequence similarity to any of the four known classes of carbonic anhydrase (alpha, beta, gamma, or delta), and so it was initially classified as belonging to a new class, epsilon. The crystal structure of CsoSCA from Halothiobacillus neapolitanus reveals that it is actually a representative member of a new subclass of beta-carbonic anhydrases, distinguished by a lack of active site pairing. Whereas a typical beta-carbonic anhydrase maintains a pair of active sites organized within a two-fold symmetric homodimer or pair of fused, homologous domains, the two domains in CsoSCA have diverged to the point that only one domain in the pair retains a viable active site. We suggest that this defunct and somewhat diminished domain has evolved a new function, specific to its carboxysomal environment. Despite the level of sequence divergence that separates CsoSCA from the other two subclasses of beta-carbonic anhydrases, there is a remarkable level of structural similarity among active site regions, which suggests a common catalytic mechanism for the interconversion of HCO(3)(-) and CO(2). Crystal packing analysis suggests that CsoSCA exists within the carboxysome shell either as a homodimer or as extended filaments.

About this StructureAbout this Structure

2FGY is a Single protein structure of sequence from Halothiobacillus neapolitanus with as ligand. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

ReferenceReference

The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two., Sawaya MR, Cannon GC, Heinhorst S, Tanaka S, Williams EB, Yeates TO, Kerfeld CA, J Biol Chem. 2006 Mar 17;281(11):7546-55. Epub 2006 Jan 10. PMID:16407248

Page seeded by OCA on Thu Feb 21 17:21:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-CsoSCA (formerly CsoS3) is a bacterial carbonic anhydrase localized in the, shell of a cellular microcompartment called the carboxysome, where it, converts HCO(3)(-) to CO(2) for use in carbon fixation by, ribulose-bisphosphate carboxylase/oxygenase (RuBisCO). CsoSCA lacks, significant sequence similarity to any of the four known classes of, carbonic anhydrase (alpha, beta, gamma, or delta), and so it was initially, classified as belonging to a new class, epsilon. The crystal structure of, CsoSCA from Halothiobacillus neapolitanus reveals that it is actually a, representative member of a new subclass of beta-carbonic anhydrases, distinguished by a lack of active site pairing. Whereas a typical, beta-carbonic anhydrase maintains a pair of active sites organized within, a two-fold symmetric homodimer or pair of fused, homologous domains, the, two domains in CsoSCA have diverged to the point that only one domain in, the pair retains a viable active site. We suggest that this defunct and, somewhat diminished domain has evolved a new function, specific to its, carboxysomal environment. Despite the level of sequence divergence that, separates CsoSCA from the other two subclasses of beta-carbonic, anhydrases, there is a remarkable level of structural similarity among, active site regions, which suggests a common catalytic mechanism for the, interconversion of HCO(3)(-) and CO(2). Crystal packing analysis suggests, that CsoSCA exists within the carboxysome shell either as a homodimer or, as extended filaments.
+CsoSCA (formerly CsoS3) is a bacterial carbonic anhydrase localized in the shell of a cellular microcompartment called the carboxysome, where it converts HCO(3)(-) to CO(2) for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase (RuBisCO). CsoSCA lacks significant sequence similarity to any of the four known classes of carbonic anhydrase (alpha, beta, gamma, or delta), and so it was initially classified as belonging to a new class, epsilon. The crystal structure of CsoSCA from Halothiobacillus neapolitanus reveals that it is actually a representative member of a new subclass of beta-carbonic anhydrases, distinguished by a lack of active site pairing. Whereas a typical beta-carbonic anhydrase maintains a pair of active sites organized within a two-fold symmetric homodimer or pair of fused, homologous domains, the two domains in CsoSCA have diverged to the point that only one domain in the pair retains a viable active site. We suggest that this defunct and somewhat diminished domain has evolved a new function, specific to its carboxysomal environment. Despite the level of sequence divergence that separates CsoSCA from the other two subclasses of beta-carbonic anhydrases, there is a remarkable level of structural similarity among active site regions, which suggests a common catalytic mechanism for the interconversion of HCO(3)(-) and CO(2). Crystal packing analysis suggests that CsoSCA exists within the carboxysome shell either as a homodimer or as extended filaments.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Halothiobacillus neapolitanus]]
 [[Category: Single protein]]
-[[Category: Sawaya, M.R.]]
+[[Category: Sawaya, M R.]]
 [[Category: ZN]]
 [[Category: beta class of carbonic anhydrase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:36:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:16 2008''