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1fp3

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[[Image:1fp3.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY==
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|PDB= 1fp3 |SIZE=350|CAPTION= <scene name='initialview01'>1fp3</scene>, resolution 2.00&Aring;
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<StructureSection load='1fp3' size='340' side='right'caption='[[1fp3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1fp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FP3 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylglucosamine_2-epimerase N-acylglucosamine 2-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.8 5.1.3.8] </span>
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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]] 2&#8491;</td></tr>
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|GENE=
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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=1fp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp3 OCA], [https://pdbe.org/1fp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fp3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fp3 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp3 OCA], [http://www.ebi.ac.uk/pdbsum/1fp3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fp3 RCSB]</span>
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[https://www.uniprot.org/uniprot/RENBP_PIG RENBP_PIG] Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY'''
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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/fp/1fp3_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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The X-ray crystallographic structure of N-acyl-d-glucosamine 2-epimerase (AGE) from porcine kidney, which has been identified to be a renin-binding protein (RnBP), was determined by the multiple isomorphous replacement method and refined at 2.0 A resolution with a final R-factor of 16.9 % for 15 to 2.0 A resolution data. The refined structure of AGE comprised 804 amino acid residues (one dimer) and 145 water molecules. The dimer of AGE had an asymmetric unit with approximate dimensions 46 Ax48 Ax96 A. The AGE monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is found in glucoamylase and cellulase. One side of the AGE alpha(6)/alpha(6)-barrel structure comprises long loops containing five short beta-sheets, and contributes to the formation of a deep cleft shaped like a funnel. The putative active-site pocket and a possible binding site for the substrate N-acetyl-d-glucosamine (GlcNAc) were found in the cleft. The other side of the alpha(6)/alpha(6)-barrel comprises short loops and contributes to the dimer formation. At the dimer interface, which is composed of the short loops and alpha-helices of the subunits, five strong ion-pair interactions were observed, which play a major role in the dimer assembly. This completely ruled out the previously accepted hypothesis that the formation of the RnBP homodimer and RnBP-renin heterodimer requires the leucine zipper motif present in RnBP.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1fp3 ConSurf].
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1FP3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FP3 OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution., Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K, J Mol Biol. 2000 Nov 10;303(5):733-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11061972 11061972]
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[[Category: Large Structures]]
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[[Category: N-acylglucosamine 2-epimerase]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Hashimoto, W.]]
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[[Category: Hashimoto W]]
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[[Category: Itoh, T.]]
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[[Category: Itoh T]]
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[[Category: Maru, I.]]
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[[Category: Maru I]]
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[[Category: Mikami, B.]]
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[[Category: Mikami B]]
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[[Category: Murata, K.]]
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[[Category: Murata K]]
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[[Category: Ohta, Y.]]
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[[Category: Ohta Y]]
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[[Category: alpha/alpha-barrel]]
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[[Category: n-acyl-d-glucosamine 2-epimerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:23 2008''
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Current revision

CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY

PDB ID 1fp3

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