1y1c

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of Anemonia elastase inhibitor analogue

Structural highlights

1y1c is a 1 chain structure with sequence from Anemonia sulcata. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IELA_ANESU

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

Anemonia elastase inhibitor (AEI) is a "nonclassical" Kazal-type elastase inhibitor from Anemonia sulcata. Unlike many nonclassical inhibitors, AEI does not have a cystine-stabilized alpha-helical (CSH) motif in the sequence. We chemically synthesized AEI and determined its three-dimensional solution structure by two-dimensional NMR spectroscopy. The resulting structure of AEI was characterized by a central alpha-helix and a three-stranded antiparallel beta-sheet of a typical Kazal-type inhibitor such as silver pheasant ovomucoid third domain (OMSVP3), even though the first and fifth half-cystine residues forming a disulfide bond in AEI are shifted both toward the C-terminus in comparison with those of OMSVP3. Synthesized AEI exhibited unexpected strong inhibition toward Streptomyces griseus protease B (SGPB). Our previous study [Hemmi, H., et al. (2003) Biochemistry 42, 2524-2534] demonstrated that the site-specific introduction of the engineered disulfide bond into the OMSVP3 molecule to form the CSH motif could produce an inhibitor with a narrower specificity. Thus, the CSH motif-containing derivative of AEI (AEI analogue) was chemically synthesized when a Cys(4)-Cys(34) bond was changed to a Cys(6)-Cys(31) bond. The AEI analogue scarcely inhibited porcine pancreatic elastase (PPE), even though it exhibited almost the same potent inhibitory activity toward SGPB. For the molecular scaffold, essentially no structural difference was detected between the two, but the N-terminal loop from Pro(5) to Ile(7) near the putative reactive site (Met(10)-Gln(11)) in the analogue moved by 3.7 A toward the central helix to form the introduced Cys(6)-Cys(31) bond. Such a conformational change in the restricted region correlates with the specificity change of the inhibitor.

Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata.,Hemmi H, Kumazaki T, Yoshizawa-Kumagaye K, Nishiuchi Y, Yoshida T, Ohkubo T, Kobayashi Y Biochemistry. 2005 Jul 19;44(28):9626-36. PMID:16008348^[1]

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

References

↑ Hemmi H, Kumazaki T, Yoshizawa-Kumagaye K, Nishiuchi Y, Yoshida T, Ohkubo T, Kobayashi Y. Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata. Biochemistry. 2005 Jul 19;44(28):9626-36. PMID:16008348 doi:10.1021/bi0472806

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://proteopedia.org/wiki/index.php/1y1c"

@@ Line 1: / Line 1: @@
 ==Solution structure of Anemonia elastase inhibitor analogue==
-<StructureSection load='1y1c' size='340' side='right' caption='[[1y1c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1y1c' size='340' side='right'caption='[[1y1c]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y1c]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y1C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y1c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anemonia_sulcata Anemonia sulcata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1C FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y1b|1y1b]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y1c RCSB], [http://www.ebi.ac.uk/pdbsum/1y1c PDBsum]</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=1y1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1c OCA], [https://pdbe.org/1y1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1c RCSB], [https://www.ebi.ac.uk/pdbsum/1y1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1c ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IELA_ANESU IELA_ANESU]
 == 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/y1/1y1c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y1c_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/chain_selection.php?pdb_ID=2ata 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=1y1c ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1y1c" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Hemmi, H.]]
+[[Category: Anemonia sulcata]]
-[[Category: Kobayashi, Y.]]
+[[Category: Large Structures]]
-[[Category: Kumazaki, T.]]
+[[Category: Hemmi H]]
-[[Category: Nishiuchi, Y.]]
+[[Category: Kobayashi Y]]
-[[Category: Ohkubo, T.]]
+[[Category: Kumazaki T]]
-[[Category: Yoshida, T.]]
+[[Category: Nishiuchi Y]]
-[[Category: Yoshizawa-Kumagaye, K.]]
+[[Category: Ohkubo T]]
-[[Category: Csh motif]]
+[[Category: Yoshida T]]
-[[Category: Hydrolase inhibitor]]
+[[Category: Yoshizawa-Kumagaye K]]
-[[Category: Kazal-type]]
-[[Category: Non-classical]]
-[[Category: Protease inhibitor]]

1y1c

From Proteopedia

Current revision

Solution structure of Anemonia elastase inhibitor analogue

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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