1h6j: Difference between revisions

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[[Image:1h6j.~~gif~~|left|200px]]

[[Image:1h6j.png|left|200px]]

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~~'''~~THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI~~'''~~

===THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI===

~~==Overview==~~

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~~CMP~~-~~Kdo synthetases from Gram~~-~~negative bacteria activate Kdo for incorporation into lipo- and capsule-polysaccharides. Here we report~~ the ~~crystal structure of~~ the ~~capsule-specific synthetase from E. coli~~ at ~~2.3 A resolution. The enzyme is a dimer of 2 x 245 amino acid residues assuming C2 symmetry~~. ~~It contains a central predominantly parallel beta-sheet with surrounding helices~~. ~~The chain fold~~ is ~~novel; it is remotely related to a double Rossmann fold. A large pocket at the carboxyl terminal ends of~~ the ~~central~~. ~~beta~~-~~strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first beta~~-~~strand and the following helix is indicated by a bound iridium hexachloride anion.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8706906}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8706906 is the PubMed ID number.

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==About this Structure==

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[[Category: Cmp-kdo synthetase]]

[[Category: Saccharide activation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:29:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:42:31 2008''

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-[[Image:1h6j.gif|left|200px]]
+{{Seed}}
+[[Image:1h6j.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1h6j|  PDB=1h6j  |  SCENE=  }}
-'''THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI'''
+===THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI===
-==Overview==
+<!--
-CMP-Kdo synthetases from Gram-negative bacteria activate Kdo for incorporation into lipo- and capsule-polysaccharides. Here we report the crystal structure of the capsule-specific synthetase from E. coli at 2.3 A resolution. The enzyme is a dimer of 2 x 245 amino acid residues assuming C2 symmetry. It contains a central predominantly parallel beta-sheet with surrounding helices. The chain fold is novel; it is remotely related to a double Rossmann fold. A large pocket at the carboxyl terminal ends of the central. beta-strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first beta-strand and the following helix is indicated by a bound iridium hexachloride anion.
+The line below this paragraph, {{ABSTRACT_PUBMED_8706906}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8706906 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8706906}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Cmp-kdo synthetase]]
 [[Category: Saccharide activation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:29:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:42:31 2008''