1fp3: Difference between revisions

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New page: left|200px<br /><applet load="1fp3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fp3, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fp3.jpg|left|200px]]<br /><applet load="1fp3" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY'''<br />


==Overview==
==CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY==
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.
<StructureSection load='1fp3' size='340' side='right'caption='[[1fp3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1FP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FP3 OCA].
</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>
 
<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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11061972 11061972]
== Function ==
[[Category: N-acylglucosamine 2-epimerase]]
[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.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fp3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Hashimoto, W.]]
[[Category: Hashimoto W]]
[[Category: Itoh, T.]]
[[Category: Itoh T]]
[[Category: Maru, I.]]
[[Category: Maru I]]
[[Category: Mikami, B.]]
[[Category: Mikami B]]
[[Category: Murata, K.]]
[[Category: Murata K]]
[[Category: Ohta, Y.]]
[[Category: Ohta Y]]
[[Category: alpha/alpha-barrel]]
[[Category: n-acyl-d-glucosamine 2-epimerase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:06:36 2007''

Latest revision as of 16:23, 13 March 2024

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

Structural highlights

1fp3 is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

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

1fp3, resolution 2.00Å

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