1ddz

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[[Image:1ddz.gif|left|200px]]<br /><applet load="1ddz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ddz.gif|left|200px]]
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caption="1ddz, resolution 2.2&Aring;" />
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'''X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1'''<br />
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{{Structure
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|PDB= 1ddz |SIZE=350|CAPTION= <scene name='initialview01'>1ddz</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|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]
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|GENE=
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}}
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'''X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DDZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10681531 10681531]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:40 2008''
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''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


PDB ID 1ddz

Drag the structure with the mouse to rotate
, resolution 2.2Å
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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