1xvm: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1xvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XVM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1xvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XVM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pq8|1pq8]], [[1pq5|1pq5]], [[1ppz|1ppz]], [[1pqa|1pqa]], [[1xvo|1xvo]]</div></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]] 1.1&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </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=1xvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvm OCA], [https://pdbe.org/1xvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xvm RCSB], [https://www.ebi.ac.uk/pdbsum/1xvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvm 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=1xvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvm OCA], [https://pdbe.org/1xvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xvm RCSB], [https://www.ebi.ac.uk/pdbsum/1xvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRYP_FUSOX TRYP_FUSOX]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Trypsin]]
[[Category: Lamzin VS]]
[[Category: Lamzin, V S]]
[[Category: Schmidt A]]
[[Category: Schmidt, A]]
[[Category: Atomic resolution]]
[[Category: Hydrolase]]
[[Category: Mobility]]
[[Category: Room temperature]]

Revision as of 11:09, 25 October 2023

Trypsin from Fusarium oxysporum- room temperature to atomic resolutionTrypsin from Fusarium oxysporum- room temperature to atomic resolution

Structural highlights

1xvm is a 2 chain structure with sequence from Fusarium oxysporum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRYP_FUSOX

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

The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.

Extraction of functional motion in trypsin crystal structures.,Schmidt A, Lamzin VS Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1132-9. Epub 2005, Jul 20. PMID:16041079[1]

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

See Also

References

  1. Schmidt A, Lamzin VS. Extraction of functional motion in trypsin crystal structures. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1132-9. Epub 2005, Jul 20. PMID:16041079 doi:10.1107/S0907444905016732

1xvm, resolution 1.10Å

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OCA