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1zrs

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(New page: 200px<br /><applet load="1zrs" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zrs, resolution 1.50&Aring;" /> '''wild-type LD-carboxy...)
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[[Image:1zrs.gif|left|200px]]<br /><applet load="1zrs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zrs, resolution 1.50&Aring;" />
 
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'''wild-type LD-carboxypeptidase'''<br />
 
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==Overview==
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==wild-type LD-carboxypeptidase==
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LD-Carboxypeptidases (EC 3.4.17.13) are named for their ability to cleave, amide bonds between l- and d-amino acids, which occur naturally in, bacterial peptidoglycan. They are specific for the link between, meso-diaminopimelic acid and d-alanine and therefore degrade GlcNAc-MurNAc, tetrapeptides to the corresponding tripeptides. As only the tripeptides, can be reused as peptidoglycan building blocks, ld-carboxypeptidases are, thought to play a role in peptidoglycan recycling. Despite the, pharmaceutical interest in peptidoglycan biosynthesis, the fold and, catalytic type of ld-carboxypeptidases are unknown. Here, we show that a, previously uncharacterized open reading frame in Pseudomonas aeruginosa, has ld-carboxypeptidase activity and present the crystal structure of this, enzyme. The structure shows that the enzyme consists of an N-terminal, beta-sheet and a C-terminal beta-barrel domain. At the interface of the, two domains, Ser(115) adopts a highly strained conformation in the context, of a strand-turn-helix motif that is similar to the "nucleophilic elbow", in alphabeta-hydrolases. Ser(115) is hydrogen-bonded to a histidine, residue, which is oriented by a glutamate residue. All three residues, which occur in the order Ser-Glu-His in the amino acid sequence, are, strictly conserved in naturally occurring ld-carboxypeptidases and cannot, be mutated to alanines without loss of activity. We conclude that, ld-carboxypeptidases are serine peptidases with Ser-His-Glu catalytic, triads.
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<StructureSection load='1zrs' size='340' side='right'caption='[[1zrs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1zrs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRS FirstGlance]. <br>
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1ZRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Active as [http://en.wikipedia.org/wiki/Muramoyltetrapeptide_carboxypeptidase Muramoyltetrapeptide carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.13 3.4.17.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRS OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrs OCA], [https://pdbe.org/1zrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zrs RCSB], [https://www.ebi.ac.uk/pdbsum/1zrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zrs ProSAT]</span></td></tr>
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==Reference==
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</table>
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Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow., Korza HJ, Bochtler M, J Biol Chem. 2005 Dec 9;280(49):40802-12. Epub 2005 Sep 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16162494 16162494]
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== Function ==
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[[Category: Muramoyltetrapeptide carboxypeptidase]]
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[https://www.uniprot.org/uniprot/LDC_PSEAE LDC_PSEAE] Releases the terminal D-alanine residue from the cytoplasmic disaccharide-tetrapeptide GlcNAc-MurNAc-L-Ala-gamma-D-Glu-meso-Dap-D-Ala, which is a murein turnover product. Probably also act on free tetrapetide. May be involved in murein recycling.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zr/1zrs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zrs ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Bochtler M]]
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[[Category: Bochtler, M.]]
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[[Category: Korza HJ]]
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[[Category: Korza, H.J.]]
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[[Category: ld-carboxypeptidase]]
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[[Category: nucleophilic elbow]]
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[[Category: peptidoglycan hydrolase]]
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[[Category: serine peptidase]]
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[[Category: serine-histidine-glutamate triad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:41:29 2008''
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Current revision

wild-type LD-carboxypeptidase

PDB ID 1zrs

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