1s44

From Proteopedia

(Difference between revisions)

Revision as of 06:12, 23 August 2023

The structure and refinement of apocrustacyanin C2 to 1.6A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.

Structural highlights

1s44 is a 2 chain structure with sequence from Homarus gammarus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CRA1_HOMGA Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster.

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 blue carotenoprotein alpha-crustacyanin of Homarus gammarus lobster carapace is comprised chemically of five 20 kDa subunits. Only two genes for the proteins have been isolated (J. B. C. Findlay, personal communication) and the five apoproteins fall into two sets of homologous proteins based on their chemical properties (CRTC, consisting of apoproteins C(1), C(2) and A(1), and CRTA, consisting of apoproteins A(2) and A(3)). The diffraction quality of apo C(2) has been improved from 2.2 to 1.3 A and its structure solved. The structure is compared with the A(1) and C(1) proteins determined at 1.4 A [Cianci et al. (2001), Acta Cryst. D57, 1219-1229] and 1.15 A, respectively [Gordon et al. (2001), Acta Cryst. D57, 1230-1237] and found to be very similar. Normalized B-factor difference plots per residue of different types were used to try to find chemically modified residues; none were found at these resolutions. It remains possible that the differences between the CRTC proteins result from differences in amidation. By comparison of a crystal grown with glycerol (studied at 1.6 A) and one grown without glycerol (studied at 1.3 A) it was seen that glycerol bound at the astaxanthin site.

The structure and refinement of apocrustacyanin C2 to 1.3 A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.,Habash J, Helliwell JR, Raftery J, Cianci M, Rizkallah PJ, Chayen NE, Nneji GA, Zagalsky PF Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):493-8. Epub 2004, Feb 25. PMID:14993674^[1]

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

References

↑ Habash J, Helliwell JR, Raftery J, Cianci M, Rizkallah PJ, Chayen NE, Nneji GA, Zagalsky PF. The structure and refinement of apocrustacyanin C2 to 1.3 A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):493-8. Epub 2004, Feb 25. PMID:14993674 doi:10.1107/S090744490400037X

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://52.214.119.220/wiki/index.php/1s44"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1s44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homarus_gammarus Homarus gammarus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S44 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s2p|1s2p]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1s44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s44 OCA], [https://pdbe.org/1s44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s44 RCSB], [https://www.ebi.ac.uk/pdbsum/1s44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s44 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CRA1_HOMGA CRA1_HOMGA]] Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster.
+[https://www.uniprot.org/uniprot/CRA1_HOMGA CRA1_HOMGA] Binds the carotenoid astaxanthin (AXT) which provides the blue coloration to the carapace of the lobster.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 [[Category: Homarus gammarus]]
 [[Category: Large Structures]]
-[[Category: Chayen, N E]]
+[[Category: Chayen NE]]
-[[Category: Cianci, M]]
+[[Category: Cianci M]]
-[[Category: Habash, J]]
+[[Category: Habash J]]
-[[Category: Helliwell, J R]]
+[[Category: Helliwell JR]]
-[[Category: Nneji, G A]]
+[[Category: Nneji GA]]
-[[Category: Raftery, J]]
+[[Category: Raftery J]]
-[[Category: Rizkallah, P J]]
+[[Category: Rizkallah PJ]]
-[[Category: Zagalsky, P F]]
+[[Category: Zagalsky PF]]
-[[Category: Crustacyanin]]
-[[Category: Glycerol]]
-[[Category: Post-translational modification]]
-[[Category: Protein binding]]
-[[Category: Refinement]]

1s44

From Proteopedia

Revision as of 06:12, 23 August 2023

The structure and refinement of apocrustacyanin C2 to 1.6A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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