2fua: Difference between revisions

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[[Image:2fua.~~jpg~~|left|200px]]

[[Image:2fua.png|left|200px]]

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~~'''~~L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT~~'''~~

===L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT===

~~==Overview==~~

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~~The structure of the class II zinc~~-~~ion dependent L~~-~~fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution.~~ The ~~homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical~~, ~~which contradicts an observed birefringence anomaly of~~ the ~~crystals. The four catalytic centers are located in deep clefts~~ at ~~the interfaces of adjacent subunits~~. ~~The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement~~. ~~In contrast to numerous other catalytically competent zinc ions~~, ~~there~~ is ~~no water molecule in~~ the ~~ligand sphere~~. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-~~ribulose~~-~~5-phosphate 4-epimerase.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15299567}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15299567 is the PubMed ID number.

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==About this Structure==

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[[Category: Schulz, G E.]]

[[Category: Class ii aldolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:19:01 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:45:40 2008''

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-[[Image:2fua.jpg|left|200px]]
+{{Seed}}
+[[Image:2fua.png|left|200px]]
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 {{STRUCTURE_2fua|  PDB=2fua  |  SCENE=  }}
-'''L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT'''
+===L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT===
-==Overview==
+<!--
-The structure of the class II zinc-ion dependent L-fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution. The homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical, which contradicts an observed birefringence anomaly of the crystals. The four catalytic centers are located in deep clefts at the interfaces of adjacent subunits. The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement. In contrast to numerous other catalytically competent zinc ions, there is no water molecule in the ligand sphere. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-ribulose-5-phosphate 4-epimerase.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299567}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299567 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299567}}
 ==About this Structure==
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 [[Category: Schulz, G E.]]
 [[Category: Class ii aldolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:19:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:45:40 2008''