1ekj: Difference between revisions
New page: left|200px<br /><applet load="1ekj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ekj, resolution 1.93Å" /> '''THE X-RAY CRYSTALLOG... |
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[[Image:1ekj.gif|left|200px]]<br /><applet load="1ekj" size=" | [[Image:1ekj.gif|left|200px]]<br /><applet load="1ekj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ekj, resolution 1.93Å" /> | caption="1ekj, resolution 1.93Å" /> | ||
'''THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM'''<br /> | '''THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM'''<br /> | ||
==Overview== | ==Overview== | ||
We have determined the structure of the beta-carbonic anhydrase from the | We have determined the structure of the beta-carbonic anhydrase from the dicotyledonous plant Pisum sativum at 1.93 A resolution, using a combination of multiple anomalous scattering off the active site zinc ion and non-crystallographic symmetry averaging. The mol- ecule assembles as an octamer with a novel dimer of dimers of dimers arrangement. Two distinct patterns of conservation of active site residues are observed, implying two potentially mechanistically distinct classes of beta-carbonic anhydrases. The active site is located at the interface between two monomers, with Cys160, His220 and Cys223 binding the catalytic zinc ion and residues Asp162 (oriented by Arg164), Gly224, Gln151, Val184, Phe179 and Tyr205 interacting with the substrate analogue, acetic acid. The substrate binding groups have a one to one correspondence with the functional groups in the alpha-carbonic anhydrase active site, with the corresponding residues being closely superimposable by a mirror plane. Therefore, despite differing folds, alpha- and beta-carbonic anhydrase have converged upon a very similar active site design and are likely to share a common mechanism. | ||
==About this Structure== | ==About this Structure== | ||
1EKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with ACT, AZI, ZN, CU, CL, CIT and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | 1EKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=AZI:'>AZI</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1EKJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kimber, M | [[Category: Kimber, M S.]] | ||
[[Category: Pai, E | [[Category: Pai, E F.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: AZI]] | [[Category: AZI]] | ||
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[[Category: strand exchange]] | [[Category: strand exchange]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:42 2008'' |