OCA at 05:53, 23 August 2023

2023-08-23T05:53:41Z

←Older revision		Revision as of 05:53, 23 August 2023
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-	'''Unreleased structure'''

-	~~The entry~~ 8f0v is ~~ON HOLD~~	+	==Lipocalin-like Milk protein-2 - E38A mutant==
		+	<StructureSection load='8f0v' size='340' side='right'caption='[[8f0v]], [[Resolution\|resolution]] 2.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8f0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Diploptera_punctata Diploptera punctata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F0V FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.951Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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=8f0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f0v OCA], [https://pdbe.org/8f0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f0v RCSB], [https://www.ebi.ac.uk/pdbsum/8f0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f0v ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q6SVB5_DIPPU Q6SVB5_DIPPU]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Diploptera punctata, also known as the Pacific beetle cockroach, is a viviparous cockroach that gives birth to live offspring and secretes a highly concentrated mixture of glycosylated proteins as a source of nourishment for developing embryos. These proteins are lipocalins that bind to lipids and crystallize in the gut of the embryo. A structure of milk crystals harvested from the embryos showed that the milk-derived crystals were heterogeneous and made of three proteins (called Lili-Mips). We hypothesized that the isoforms of Lili-Mip would display different affinities for fatty acids due to the ability of the pocket to bind multiple acyl chain lengths. We previously reported the structures of Lili-Mip from crystals grown in vivo and recombinantly expressed Lili-Mip2. These structures are similar, and both bind to several fatty acids. This study explores the specificity and affinity of fatty acid binding to recombinantly expressed Lili-Mip 1, 2 & 3. We show that all isoforms can bind to different fatty acids with similar affinities. We also report the thermostability of Lili-Mip is pH dependent, where stability is highest at acidic pH and declines as the pH increases to physiological levels near 7.0. We show that thermostability is an inherent property of the protein, and glycosylation and ligand binding do not change it significantly. Measuring the pH in the embryo's gut lumen and gut cells suggests that the pH in the gut is acidic and the pH inside the gut cells is closer to neutral pH. In various crystal structures (reported here and previously by us), Phe-98 and Phe-100 occupy multiple conformations in the binding pocket. In our earlier work, we had shown that the loops at the entrance could adapt various conformations to change the size of the binding pocket. Here we show Phe-98 and Phe-100 can reorient to stabilize interactions at the bottom of the cavity-and change the volume of the cavity from 510 A3 to 337 A3. Together they facilitate the binding of fatty acids of different acyl chain lengths.

-	~~Authors: Subramanian~~, R., ~~KanagaVijayan, D~~.	+	Variability in phenylalanine side chain conformations facilitates broad substrate tolerance of fatty acid binding in cockroach milk proteins.,Santhakumari PR, Dhanabalan K, Virani S, Hopf-Jannasch AS, Benoit JB, Chopra G, Subramanian R PLoS One. 2023 Jun 29;18(6):e0280009. doi: 10.1371/journal.pone.0280009. , eCollection 2023. PMID:37384723<ref>PMID:37384723</ref>

-	~~Description: Lipocalin-like Milk protein~~-2 -~~E38A mutant~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Kanagavijayan,~~ D]]	+	<div class="pdbe-citations 8f0v" style="background-color:#fffaf0;"></div>
-	[[Category: Subramanian, R]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Diploptera punctata]]
		+	[[Category: Large Structures]]
		+	[[Category: KanagaVijayan D]]
		+	[[Category: Subramanian R]]

OCA: Protected "8f0v" [edit=sysop:move=sysop]

2022-11-09T05:09:55Z

Protected "8f0v" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:09, 9 November 2022

OCA: New page: '''Unreleased structure''' The entry 8f0v is ON HOLD Authors: Subramanian, R., KanagaVijayan, D. Description: Lipocalin-like Milk protein-2 -E38A mutant [[Category: Unreleased Structur...

2022-11-09T05:09:54Z

New page: '''Unreleased structure''' The entry 8f0v is ON HOLD Authors: Subramanian, R., KanagaVijayan, D. Description: Lipocalin-like Milk protein-2 -E38A mutant [[Category: Unreleased Structur...

New page

'''Unreleased structure'''

The entry 8f0v is ON HOLD

Authors: Subramanian, R., KanagaVijayan, D.

Description: Lipocalin-like Milk protein-2 -E38A mutant
[[Category: Unreleased Structures]]
[[Category: Kanagavijayan, D]]
[[Category: Subramanian, R]]

8f0v - Revision history

OCA at 05:53, 23 August 2023

OCA: Protected "8f0v" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 8f0v is ON HOLD Authors: Subramanian, R., KanagaVijayan, D. Description: Lipocalin-like Milk protein-2 -E38A mutant [[Category: Unreleased Structur...