3isz

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{{STRUCTURE_3isz| PDB=3isz | SCENE= }}
{{STRUCTURE_3isz| PDB=3isz | SCENE= }}
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===Crystal structure of mono-zinc form of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae===
===Crystal structure of mono-zinc form of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae===
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{{ABSTRACT_PUBMED_20138056}}
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==Function==
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[[http://www.uniprot.org/uniprot/DAPE_HAEIN DAPE_HAEIN]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. It can only hydrolyze L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive toward D,L-, L,D-, and D,D-SDAP.<ref>PMID:12962500</ref><ref>PMID:16421726</ref><ref>PMID:18712420</ref>
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{{ABSTRACT_PUBMED_20138056}}
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==About this Structure==
==About this Structure==
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3ISZ is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ISZ OCA].
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[[3isz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ISZ OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20138056</ref><references group="xtra"/>
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<ref group="xtra">PMID:020138056</ref><references group="xtra"/><references/>
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[[Category: Haemophilus influenzae rd kw20]]
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[[Category: Haemophilus influenzae]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Gillner, D M.]]
[[Category: Gillner, D M.]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
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[[Category: Zinc]]
 
[[Category: Zn-binding]]
[[Category: Zn-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:01:46 2010''
 

Revision as of 09:31, 27 March 2013

Template:STRUCTURE 3isz

Contents

Crystal structure of mono-zinc form of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae

Template:ABSTRACT PUBMED 20138056

Function

[DAPE_HAEIN] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. It can only hydrolyze L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive toward D,L-, L,D-, and D,D-SDAP.[1][2][3]

About this Structure

3isz is a 2 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

  • Nocek BP, Gillner DM, Fan Y, Holz RC, Joachimiak A. Structural basis for catalysis by the mono- and dimetalated forms of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase. J Mol Biol. 2010 Apr 2;397(3):617-26. Epub 2010 Feb 4. PMID:20138056 doi:10.1016/j.jmb.2010.01.062
  1. ↑ Bienvenue DL, Gilner DM, Davis RS, Bennett B, Holz RC. Substrate specificity, metal binding properties, and spectroscopic characterization of the DapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae. Biochemistry. 2003 Sep 16;42(36):10756-63. PMID:12962500 doi:http://dx.doi.org/10.1021/bi034845+
  2. ↑ Davis R, Bienvenue D, Swierczek SI, Gilner DM, Rajagopal L, Bennett B, Holz RC. Kinetic and spectroscopic characterization of the E134A- and E134D-altered dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae. J Biol Inorg Chem. 2006 Mar;11(2):206-16. Epub 2006 Jan 19. PMID:16421726 doi:10.1007/s00775-005-0071-8
  3. ↑ Gillner DM, Bienvenue DL, Nocek BP, Joachimiak A, Zachary V, Bennett B, Holz RC. The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues. J Biol Inorg Chem. 2009 Jan;14(1):1-10. doi: 10.1007/s00775-008-0418-z. Epub 2008, Aug 19. PMID:18712420 doi:10.1007/s00775-008-0418-z

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