1ddz
From Proteopedia
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- | [[Image:1ddz.gif|left|200px]] | + | [[Image:1ddz.gif|left|200px]] |
- | + | ||
- | '''X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1''' | + | {{Structure |
+ | |PDB= 1ddz |SIZE=350|CAPTION= <scene name='initialview01'>1ddz</scene>, resolution 2.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DDZ is a [ | + | 1DDZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum]. The following page contains interesting information on the relation of 1DDZ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb49_1.html Carbonic Anhydrase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA]. |
==Reference== | ==Reference== | ||
- | X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration., Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T, J Biol Chem. 2000 Feb 25;275(8):5521-6. PMID:[http:// | + | X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration., Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T, J Biol Chem. 2000 Feb 25;275(8):5521-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10681531 10681531] |
[[Category: Carbonate dehydratase]] | [[Category: Carbonate dehydratase]] | ||
[[Category: Carbonic Anhydrase]] | [[Category: Carbonic Anhydrase]] | ||
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[[Category: alpha-beta-alpha]] | [[Category: alpha-beta-alpha]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:36:56 2008'' |
Revision as of 08:36, 20 March 2008
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, resolution 2.2Å | |||||||
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Ligands: | |||||||
Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1
Overview
The carbonic anhydrases (CAs) fall into three evolutionarily distinct families designated alpha-, beta-, and gamma-CAs based on their primary structure. beta-CAs are present in higher plants, algae, and prokaryotes, and are involved in inorganic carbon utilization. Here, we describe the novel x-ray structure of beta-CA from the red alga, Porphyridium purpureum, at 2.2-A resolution using intrinsic zinc multiwavelength anomalous diffraction phasing. The CA monomer is composed of two internally repeating structures, being folded as a pair of fundamentally equivalent motifs of an alpha/beta domain and three projecting alpha-helices. The motif is obviously distinct from that of either alpha- or gamma-CAs. This homodimeric CA appears like a tetramer with a pseudo 222 symmetry. The active site zinc is coordinated by a Cys-Asp-His-Cys tetrad that is strictly conserved among the beta-CAs. No water molecule is found in a zinc-liganding radius, indicating that the zinc-hydroxide mechanism in alpha-CAs, and possibly in gamma-CAs, is not directly applicable to the case in beta-CAs. Zinc coordination environments of the CAs provide an interesting example of the convergent evolution of distinct catalytic sites required for the same CO(2) hydration reaction.
About this Structure
1DDZ is a Single protein structure of sequence from Porphyridium purpureum. The following page contains interesting information on the relation of 1DDZ with [Carbonic Anhydrase]. Full crystallographic information is available from OCA.
Reference
X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration., Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T, J Biol Chem. 2000 Feb 25;275(8):5521-6. PMID:10681531
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