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New page: left|200px<br /> <applet load="1ddz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddz, resolution 2.2Å" /> '''X-RAY STRUCTURE OF A...
 
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[[Image:1ddz.gif|left|200px]]<br />
<applet load="1ddz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ddz, resolution 2.2&Aring;" />
'''X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1'''<br />


==Overview==
==X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1==
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.
<StructureSection load='1ddz' size='340' side='right'caption='[[1ddz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ddz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum]. The January 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Carbonic Anhydrase''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_1 10.2210/rcsb_pdb/mom_2004_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DDZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ddz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddz OCA], [https://pdbe.org/1ddz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ddz RCSB], [https://www.ebi.ac.uk/pdbsum/1ddz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ddz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q43060_PORPP Q43060_PORPP]


==About this Structure==
==See Also==
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 ZN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDZ OCA].
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Carbonate dehydratase]]
[[Category: Carbonic Anhydrase]]
[[Category: Carbonic Anhydrase]]
[[Category: Large Structures]]
[[Category: Porphyridium purpureum]]
[[Category: Porphyridium purpureum]]
[[Category: Single protein]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Mitsuhashi, S.]]
[[Category: Mitsuhashi S]]
[[Category: Miyachi, S.]]
[[Category: Miyachi S]]
[[Category: Mizushima, T.]]
[[Category: Mizushima T]]
[[Category: Tsukihara, T.]]
[[Category: Tsukihara T]]
[[Category: Yamashita, E.]]
[[Category: Yamashita E]]
[[Category: ZN]]
[[Category: alpha-beta-alpha]]
 
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Latest revision as of 06:52, 7 February 2024

X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1

1ddz, resolution 2.20Å

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