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.

1bwz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:20, 29 November 2017

DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE

Structural highlights

1bwz is a 1 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DAPF ("Bacterium influenzae" Lehmann and Neumann 1896)
Activity:	Diaminopimelate epimerase, with EC number 5.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DAPF_HAEIN] Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Haemophilus influenzae diaminopimelate epimerase was cloned, expressed, purified, and crystallized in the C2221 space group (a = 102.1 A, b = 115.4 A, c = 66.3 A, alpha = beta = gamma = 90 degrees). The three-dimensional structure was solved to 2.7 A using a single Pt derivative and the Se-Met-substituted enzyme to a conventional R factor of 19.0% (Rfree = 24.2%). The 274 amino acid enzyme consists of two structurally homologous domains, each containing eight beta-strands and two alpha-helices. Diaminopimelate epimerase is a representative of the PLP-independent amino acid racemases, for which no structure has yet been determined and substantial evidence exists supporting the role of two cysteine residues as the catalytic acid and base. Cys73 of the amino terminal domain is found in disulfide linkage, at the domain interface, with Cys217 of the carboxy terminal domain, and we suggest that these two cysteine residues in the reduced, active enzyme function as the acid and base in the mechanism.

Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase.,Cirilli M, Zheng R, Scapin G, Blanchard JS Biochemistry. 1998 Nov 24;37(47):16452-8. PMID:9843410^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Koo CW, Blanchard JS. Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 1999 Apr 6;38(14):4416-22. PMID:10194362 doi:http://dx.doi.org/10.1021/bi982911f
↑ Cirilli M, Zheng R, Scapin G, Blanchard JS. Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 1998 Nov 24;37(47):16452-8. PMID:9843410 doi:10.1021/bi982138o

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bwz"

@@ Line 1: / Line 1: @@
 ==DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE==
 <StructureSection load='1bwz' size='340' side='right' caption='[[1bwz]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAPF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diaminopimelate_epimerase Diaminopimelate epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.7 5.1.1.7] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwz OCA], [http://pdbe.org/1bwz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bwz RCSB], [http://www.ebi.ac.uk/pdbsum/1bwz PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwz OCA], [http://pdbe.org/1bwz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bwz RCSB], [http://www.ebi.ac.uk/pdbsum/1bwz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwz ProSAT]</span></td></tr>
 </table>
 == Function ==

1bwz

From Proteopedia

Revision as of 08:20, 29 November 2017

DIAMINOPIMELATE EPIMERASE FROM HEMOPHILUS INFLUENZAE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox