This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3isz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3isz.png|left|200px]]
 
- 
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_3isz", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_3isz| PDB=3isz | SCENE= }}
{{STRUCTURE_3isz| PDB=3isz | SCENE= }}
- 
===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===
 +
{{ABSTRACT_PUBMED_20138056}}
-
 
+
==Function==
-
<!--
+
[[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>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20138056}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 20138056 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_20138056}}
+
==About this Structure==
==About this Structure==
-
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].
+
[[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==
-
<ref group="xtra">PMID:20138056</ref><references group="xtra"/>
+
<ref group="xtra">PMID:020138056</ref><references group="xtra"/><references/>
-
[[Category: Haemophilus influenzae rd kw20]]
+
[[Category: Haemophilus influenzae]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Gillner, D M.]]
[[Category: Gillner, D M.]]
Line 45: Line 32:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
[[Category: Succinyl-diaminopimelate desuccinylase]]
-
[[Category: Zinc]]
 
[[Category: Zn-binding]]
[[Category: Zn-binding]]
- 
-
''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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools