1i1i: Difference between revisions

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<StructureSection load='1i1i' size='340' side='right'caption='[[1i1i]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1i1i' size='340' side='right'caption='[[1i1i]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i1i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1I FirstGlance]. <br>
<table><tr><td colspan='2'>[[1i1i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Neurolysin Neurolysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.16 3.4.24.16] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1i1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1i OCA], [https://pdbe.org/1i1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1i RCSB], [https://www.ebi.ac.uk/pdbsum/1i1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1i ProSAT]</span></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=1i1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1i OCA], [https://pdbe.org/1i1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1i RCSB], [https://www.ebi.ac.uk/pdbsum/1i1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NEUL_RAT NEUL_RAT]] Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.  
[https://www.uniprot.org/uniprot/NEUL_RAT NEUL_RAT] Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1i1i ConSurf].
</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=1i1i ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow channel. This architecture accounts for specialization of this neuropeptidase to small bioactive peptide substrates without bulky secondary and tertiary structures. In addition, modeling studies indicate that the length of a substrate N-terminal to the site of hydrolysis is restricted to approximately 10 residues by the limited size of the active site cavity. Some structural elements of neurolysin, including a five-stranded beta-sheet and the two active site helices, are conserved with other metallopeptidases. The connecting loop regions of these elements, however, are much extended in neurolysin, and they, together with other open coil elements, line the active site cavity. These potentially flexible elements may account for the ability of the enzyme to cleave a variety of sequences.
Structure of neurolysin reveals a deep channel that limits substrate access.,Brown CK, Madauss K, Lian W, Beck MR, Tolbert WD, Rodgers DW Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3127-32. Epub 2001 Mar 6. PMID:11248043<ref>PMID:11248043</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i1i" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Neurolysin]]
[[Category: Rattus norvegicus]]
[[Category: Beck, M R]]
[[Category: Beck MR]]
[[Category: Brown, C K]]
[[Category: Brown CK]]
[[Category: Lian, W]]
[[Category: Lian W]]
[[Category: Madauss, K]]
[[Category: Madauss K]]
[[Category: Rodgers, D W]]
[[Category: Rodgers DW]]
[[Category: Tolbert, W D]]
[[Category: Tolbert WD]]
[[Category: Endopeptidase]]
[[Category: Hydrolase]]
[[Category: Neuropeptidase]]
[[Category: Zinc metallopeptidase]]

Latest revision as of 07:31, 7 February 2024

NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE

1i1i, resolution 2.30Å

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