The crystal structures of native and ( S )‐lysine‐bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance

The crystal structures of native and ( S )‐lysine‐bound dihydrodipicolinate synthase from... Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)‐lysine and meso‐diaminopimelate. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)‐lysine. The crystal structure of DHDPS from Escherichia coli has previously been published, but to only a resolution of 2.5 Å, and the structure of the lysine‐bound adduct was known to only 2.94 Å resolution. Here, the crystal structures of native and (S)‐lysine‐bound dihydrodipicolinate synthase from E. coli are presented to 1.9 and 2.0 Å, respectively, resolutions that allow, in particular, more accurate definition of the protein structure. The general architecture of the active site is found to be consistent with previously determined structures, but with some important differences. Arg138, which is situated at the entrance of the active site and is thought to be involved in substrate binding, has an altered conformation and is connected via a water molecule to Tyr133 of the active‐site catalytic triad. This suggests a hitherto unknown function for Arg138 in the DHDPS mechanism. Additionally, a re‐evaluation of the dimer–dimer interface reveals a more extensive network of interactions than first thought. Of particular interest is the higher resolution structure of DHDPS with (S)‐lysine bound at the allosteric site, which is remote to the active site, although connected to it by a chain of conserved water molecules. (S)‐Lysine has a slightly altered conformation from that originally determined and does not appear to alter the DHDPS structure as others have reported. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

The crystal structures of native and ( S )‐lysine‐bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance

Loading next page...
 
/lp/wiley/the-crystal-structures-of-native-and-s-lysine-bound-pBv8SfIEnW
Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
D.O.I.
10.1107/S0907444905016318
Publisher site
See Article on Publisher Site

Abstract

Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)‐lysine and meso‐diaminopimelate. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)‐lysine. The crystal structure of DHDPS from Escherichia coli has previously been published, but to only a resolution of 2.5 Å, and the structure of the lysine‐bound adduct was known to only 2.94 Å resolution. Here, the crystal structures of native and (S)‐lysine‐bound dihydrodipicolinate synthase from E. coli are presented to 1.9 and 2.0 Å, respectively, resolutions that allow, in particular, more accurate definition of the protein structure. The general architecture of the active site is found to be consistent with previously determined structures, but with some important differences. Arg138, which is situated at the entrance of the active site and is thought to be involved in substrate binding, has an altered conformation and is connected via a water molecule to Tyr133 of the active‐site catalytic triad. This suggests a hitherto unknown function for Arg138 in the DHDPS mechanism. Additionally, a re‐evaluation of the dimer–dimer interface reveals a more extensive network of interactions than first thought. Of particular interest is the higher resolution structure of DHDPS with (S)‐lysine bound at the allosteric site, which is remote to the active site, although connected to it by a chain of conserved water molecules. (S)‐Lysine has a slightly altered conformation from that originally determined and does not appear to alter the DHDPS structure as others have reported.

Journal

Acta Crystallographica Section DWiley

Published: Aug 1, 2005

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off