1h6j

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(New page: 200px<br /><applet load="1h6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6j, resolution 2.32&Aring;" /> '''THE THREE-DIMENSIONA...)
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[[Image:1h6j.gif|left|200px]]<br /><applet load="1h6j" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1h6j, resolution 2.32&Aring;" />
caption="1h6j, resolution 2.32&Aring;" />
'''THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI'''<br />
'''THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1H6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6J OCA].
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1H6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6J OCA].
==Reference==
==Reference==
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[[Category: Jann, K.]]
[[Category: Jann, K.]]
[[Category: Jelakovic, S.]]
[[Category: Jelakovic, S.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
[[Category: capsular polysaccharide]]
[[Category: capsular polysaccharide]]
[[Category: cmp-kdo synthetase]]
[[Category: cmp-kdo synthetase]]
[[Category: saccharide activation]]
[[Category: saccharide activation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:26:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:57 2008''

Revision as of 10:58, 21 February 2008


1h6j, resolution 2.32Å

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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.

About this Structure

1H6J is a Single protein structure of sequence from Escherichia coli. Active as 3-deoxy-manno-octulosonate cytidylyltransferase, with EC number 2.7.7.38 Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli., Jelakovic S, Jann K, Schulz GE, FEBS Lett. 1996 Aug 5;391(1-2):157-61. PMID:8706906

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