This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1atb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1atb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1atb" /> '''HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN...)
Current revision (15:28, 13 March 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1atb.gif|left|200px]]<br /><applet load="1atb" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1atb" />
 
-
'''HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE'''<br />
 
-
==Overview==
+
==HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE==
-
BACKGROUND: The Ascaris trypsin inhibitor (ATI) is a member of a new, family of serine protease inhibitors isolated from the helminthic worm, Ascaris lumbricoides var suum. This family comprises five, chymotrypsin/elastase inhibitors and one trypsin inhibitor. Members are, characterized by the presence of five disulfide bonds (two of which are, located on either side of the reactive site) in a single small protein, domain of 61-62 residues. RESULTS: The solution structure of ATI has been, determined at pH 2.4 and pH 4.75 by NMR spectroscopy. Iterative refinement, permitted the unambiguous assignment of the pairing of the five disulfide, bridges (Cys5-Cys38, Cys15-Cys33, Cys18-Cys29, Cys22-Cys60, and, Cys40-Cys54) which were previously unknown. The structure includes four, short beta-strands arranged in two approximately perpendicular, beta-sheets. The reactive site loop is bounded by two disulfide bridges, (Cys15-Cys33 and Cys18-Cys29) and is part of the long loop (residues, 15-25) connecting strands beta 1 and beta 2. Comparison of the nuclear, Overhauser enhancement data at the two pH values revealed significant, differences centered around the reactive site. While the reactive site at, pH 2.4 closely resembles that of other protease inhibitors, at pH 4.75 the, reactive site loop undergoes a major conformational rearrangement, involving the psi backbone torsion angles of the P2, P1 and P1' residues, (residues 30-32). This is associated with a change in the positions of the, side chains of Arg31 and Glu32. CONCLUSIONS: The overall three-dimensional, structure of ATI posesses an unusual fold and, with the exception of the, reactive site, shows no similarity to other serine protease inhibitors., The observation that the reactive site of the low pH form of ATI is, similar to that of other serine proteases suggests that this is the active, form of the protein.
+
<StructureSection load='1atb' size='340' side='right'caption='[[1atb]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1atb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATB FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1atb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atb OCA], [https://pdbe.org/1atb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1atb RCSB], [https://www.ebi.ac.uk/pdbsum/1atb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1atb ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ITR1_ASCSU ITR1_ASCSU]
 +
== 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/at/1atb_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=1atb ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1ATB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ATB OCA].
+
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site., Grasberger BL, Clore GM, Gronenborn AM, Structure. 1994 Jul 15;2(7):669-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7922043 7922043]
+
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Clore, G.M.]]
+
[[Category: Clore GM]]
-
[[Category: Grasberger, B.L.]]
+
[[Category: Grasberger BL]]
-
[[Category: Gronenborn, A.M.]]
+
[[Category: Gronenborn AM]]
-
[[Category: proteinase inhibitor(trypsin)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:07:16 2007''
+

Current revision

HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE

PDB ID 1atb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1atb"
Personal tools